recombinant toxin bekm 1  (Alomone Labs)


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    Structured Review

    Alomone Labs recombinant toxin bekm 1
    The fluorescent <t>BeKm-1</t> analogues potently inhibit hERG currents. A) Typical traces of currents recorded in Xenopus laevis oocytes that express hERG. Currents were elicited using the protocol depicted at the top in which a pulse from a holding potential of −80 mV to −30 mV precedes a test pulse at −50 mV, in the presence of increasing concentrations of native BeKm-1, Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 or Cy5-PEG5-BeKm1-Lys 27 . Scale bars, 200 nA. B) Inhibition curves of native BeKm-1 and its four analogues. The peak current amplitude was measured during the test pulse at −50 mV in the presence of toxin (ITx) and normalized to the current recorded in the absence of toxin (ICt). Data are the mean ± SEM of n = 4–10 oocytes.
    Recombinant Toxin Bekm 1, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 91/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant toxin bekm 1/product/Alomone Labs
    Average 91 stars, based on 2 article reviews
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    recombinant toxin bekm 1 - by Bioz Stars, 2022-12
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    Images

    1) Product Images from "Fluorescent analogues of BeKm-1 with high and specific activity against the hERG channel"

    Article Title: Fluorescent analogues of BeKm-1 with high and specific activity against the hERG channel

    Journal: Toxicon: X

    doi: 10.1016/j.toxcx.2019.100010

    The fluorescent BeKm-1 analogues potently inhibit hERG currents. A) Typical traces of currents recorded in Xenopus laevis oocytes that express hERG. Currents were elicited using the protocol depicted at the top in which a pulse from a holding potential of −80 mV to −30 mV precedes a test pulse at −50 mV, in the presence of increasing concentrations of native BeKm-1, Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 or Cy5-PEG5-BeKm1-Lys 27 . Scale bars, 200 nA. B) Inhibition curves of native BeKm-1 and its four analogues. The peak current amplitude was measured during the test pulse at −50 mV in the presence of toxin (ITx) and normalized to the current recorded in the absence of toxin (ICt). Data are the mean ± SEM of n = 4–10 oocytes.
    Figure Legend Snippet: The fluorescent BeKm-1 analogues potently inhibit hERG currents. A) Typical traces of currents recorded in Xenopus laevis oocytes that express hERG. Currents were elicited using the protocol depicted at the top in which a pulse from a holding potential of −80 mV to −30 mV precedes a test pulse at −50 mV, in the presence of increasing concentrations of native BeKm-1, Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 or Cy5-PEG5-BeKm1-Lys 27 . Scale bars, 200 nA. B) Inhibition curves of native BeKm-1 and its four analogues. The peak current amplitude was measured during the test pulse at −50 mV in the presence of toxin (ITx) and normalized to the current recorded in the absence of toxin (ICt). Data are the mean ± SEM of n = 4–10 oocytes.

    Techniques Used: Inhibition

    The mutation S631C in hERG decreases the affinity of native BeKm-1 and of its four fluorescent analogues for the channel. Comparison of the inhibition curves of native BeKm-1 and its four analogues Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 obtained in Xenopus laevis oocytes that express wild type (WT) hERG or the mutant S631C. The data obtained with the mutant channel were fitted by hand for the purpose of comparison. Data are the mean ± SEM of n = 3–5 oocytes.
    Figure Legend Snippet: The mutation S631C in hERG decreases the affinity of native BeKm-1 and of its four fluorescent analogues for the channel. Comparison of the inhibition curves of native BeKm-1 and its four analogues Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 obtained in Xenopus laevis oocytes that express wild type (WT) hERG or the mutant S631C. The data obtained with the mutant channel were fitted by hand for the purpose of comparison. Data are the mean ± SEM of n = 3–5 oocytes.

    Techniques Used: Mutagenesis, Inhibition

    The fluorescent BeKm-1 analogues do not affect hKv10.1 and hKv1.3 currents. A) Typical traces of currents elicited by a step depolarization to 0 mV or 70 mV, from a holding potential of −80 mV, obtained from Xenopus laevis oocytes that express hKv10.1 or hKv1.3, respectively, in the absence or presence of 200 nM native BeKm-1 and in the absence or presence of 500 nM of Cy5-PEG3-linker4-BeKm-1, of Cy5-spacerGS-linker6-BeKm-1, of Cy5-PEG5-linker10-BeKm-1 and of Cy5-PEG5-BeKm1-Lys 27 . Note the lack of effect of BeKm-1 and of the four analogues on both channels. B) Percentage of current remaining in the presence of a single dose of native BeKm-1 or its four analogues (Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 ). Current amplitude was measured before (ICt) and during (Itx) the perfusion of the different toxins. Data are the mean ± SEM of n = 4–7 oocytes.
    Figure Legend Snippet: The fluorescent BeKm-1 analogues do not affect hKv10.1 and hKv1.3 currents. A) Typical traces of currents elicited by a step depolarization to 0 mV or 70 mV, from a holding potential of −80 mV, obtained from Xenopus laevis oocytes that express hKv10.1 or hKv1.3, respectively, in the absence or presence of 200 nM native BeKm-1 and in the absence or presence of 500 nM of Cy5-PEG3-linker4-BeKm-1, of Cy5-spacerGS-linker6-BeKm-1, of Cy5-PEG5-linker10-BeKm-1 and of Cy5-PEG5-BeKm1-Lys 27 . Note the lack of effect of BeKm-1 and of the four analogues on both channels. B) Percentage of current remaining in the presence of a single dose of native BeKm-1 or its four analogues (Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 ). Current amplitude was measured before (ICt) and during (Itx) the perfusion of the different toxins. Data are the mean ± SEM of n = 4–7 oocytes.

    Techniques Used:

    Docking of BeKm-1 in a model of hERG channel and fluorescent BeKm-1 analogues used in this study. A) Left, BeKm-1 (pdb code: 1j5, magenta, top) in interaction with hERG channel (in solid ribbon representation showing the solvent surface colored by hydrophobicity). The tetrameric model of the hERG channel was generated from the pdb structure (5VA1) using the Prepare Protein module within Discovery Studio. The transmembrane domain, the cytoplasmic N-terminal Per-Arnt-Sim (PAS) domain, the C-terminal C-linker and the cyclic nucleotide binding domain (CNBD) are indicated. Docking of BeKm-1 was performed using the ZDOCK rigid body docking program and refined with the RDOCK module. The top ranked pose of the most populated cluster from the protein-protein interaction predictions is showed with BeKm-1 docked at the top of the transmembrane domain of hERG. Right, Details of the pose of BeKm-1 (magenta) within the interaction surface of hERG colored according to the Solvent Accessibility Surface (SAS) (see Supplementary Data S2), with the side chain of the N terminal Arg 1 and Arg 27 (red) and the more buried C terminal Phe 36 (orange). B) Chemical structures of fluorescent BeKm-1 analogues used in this study with different types of linkers grafted on the N-ter of Arg 1 or the side chain of Arg 27 mutated for a Lysine. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
    Figure Legend Snippet: Docking of BeKm-1 in a model of hERG channel and fluorescent BeKm-1 analogues used in this study. A) Left, BeKm-1 (pdb code: 1j5, magenta, top) in interaction with hERG channel (in solid ribbon representation showing the solvent surface colored by hydrophobicity). The tetrameric model of the hERG channel was generated from the pdb structure (5VA1) using the Prepare Protein module within Discovery Studio. The transmembrane domain, the cytoplasmic N-terminal Per-Arnt-Sim (PAS) domain, the C-terminal C-linker and the cyclic nucleotide binding domain (CNBD) are indicated. Docking of BeKm-1 was performed using the ZDOCK rigid body docking program and refined with the RDOCK module. The top ranked pose of the most populated cluster from the protein-protein interaction predictions is showed with BeKm-1 docked at the top of the transmembrane domain of hERG. Right, Details of the pose of BeKm-1 (magenta) within the interaction surface of hERG colored according to the Solvent Accessibility Surface (SAS) (see Supplementary Data S2), with the side chain of the N terminal Arg 1 and Arg 27 (red) and the more buried C terminal Phe 36 (orange). B) Chemical structures of fluorescent BeKm-1 analogues used in this study with different types of linkers grafted on the N-ter of Arg 1 or the side chain of Arg 27 mutated for a Lysine. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

    Techniques Used: Generated, Binding Assay

    2) Product Images from "Fluorescent analogues of BeKm-1 with high and specific activity against the hERG channel"

    Article Title: Fluorescent analogues of BeKm-1 with high and specific activity against the hERG channel

    Journal: Toxicon: X

    doi: 10.1016/j.toxcx.2019.100010

    The fluorescent BeKm-1 analogues potently inhibit hERG currents. A) Typical traces of currents recorded in Xenopus laevis oocytes that express hERG. Currents were elicited using the protocol depicted at the top in which a pulse from a holding potential of −80 mV to −30 mV precedes a test pulse at −50 mV, in the presence of increasing concentrations of native BeKm-1, Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 or Cy5-PEG5-BeKm1-Lys 27 . Scale bars, 200 nA. B) Inhibition curves of native BeKm-1 and its four analogues. The peak current amplitude was measured during the test pulse at −50 mV in the presence of toxin (ITx) and normalized to the current recorded in the absence of toxin (ICt). Data are the mean ± SEM of n = 4–10 oocytes.
    Figure Legend Snippet: The fluorescent BeKm-1 analogues potently inhibit hERG currents. A) Typical traces of currents recorded in Xenopus laevis oocytes that express hERG. Currents were elicited using the protocol depicted at the top in which a pulse from a holding potential of −80 mV to −30 mV precedes a test pulse at −50 mV, in the presence of increasing concentrations of native BeKm-1, Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 or Cy5-PEG5-BeKm1-Lys 27 . Scale bars, 200 nA. B) Inhibition curves of native BeKm-1 and its four analogues. The peak current amplitude was measured during the test pulse at −50 mV in the presence of toxin (ITx) and normalized to the current recorded in the absence of toxin (ICt). Data are the mean ± SEM of n = 4–10 oocytes.

    Techniques Used: Inhibition

    The mutation S631C in hERG decreases the affinity of native BeKm-1 and of its four fluorescent analogues for the channel. Comparison of the inhibition curves of native BeKm-1 and its four analogues Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 obtained in Xenopus laevis oocytes that express wild type (WT) hERG or the mutant S631C. The data obtained with the mutant channel were fitted by hand for the purpose of comparison. Data are the mean ± SEM of n = 3–5 oocytes.
    Figure Legend Snippet: The mutation S631C in hERG decreases the affinity of native BeKm-1 and of its four fluorescent analogues for the channel. Comparison of the inhibition curves of native BeKm-1 and its four analogues Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 obtained in Xenopus laevis oocytes that express wild type (WT) hERG or the mutant S631C. The data obtained with the mutant channel were fitted by hand for the purpose of comparison. Data are the mean ± SEM of n = 3–5 oocytes.

    Techniques Used: Mutagenesis, Inhibition

    The fluorescent BeKm-1 analogues do not affect hKv10.1 and hKv1.3 currents. A) Typical traces of currents elicited by a step depolarization to 0 mV or 70 mV, from a holding potential of −80 mV, obtained from Xenopus laevis oocytes that express hKv10.1 or hKv1.3, respectively, in the absence or presence of 200 nM native BeKm-1 and in the absence or presence of 500 nM of Cy5-PEG3-linker4-BeKm-1, of Cy5-spacerGS-linker6-BeKm-1, of Cy5-PEG5-linker10-BeKm-1 and of Cy5-PEG5-BeKm1-Lys 27 . Note the lack of effect of BeKm-1 and of the four analogues on both channels. B) Percentage of current remaining in the presence of a single dose of native BeKm-1 or its four analogues (Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 ). Current amplitude was measured before (ICt) and during (Itx) the perfusion of the different toxins. Data are the mean ± SEM of n = 4–7 oocytes.
    Figure Legend Snippet: The fluorescent BeKm-1 analogues do not affect hKv10.1 and hKv1.3 currents. A) Typical traces of currents elicited by a step depolarization to 0 mV or 70 mV, from a holding potential of −80 mV, obtained from Xenopus laevis oocytes that express hKv10.1 or hKv1.3, respectively, in the absence or presence of 200 nM native BeKm-1 and in the absence or presence of 500 nM of Cy5-PEG3-linker4-BeKm-1, of Cy5-spacerGS-linker6-BeKm-1, of Cy5-PEG5-linker10-BeKm-1 and of Cy5-PEG5-BeKm1-Lys 27 . Note the lack of effect of BeKm-1 and of the four analogues on both channels. B) Percentage of current remaining in the presence of a single dose of native BeKm-1 or its four analogues (Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 ). Current amplitude was measured before (ICt) and during (Itx) the perfusion of the different toxins. Data are the mean ± SEM of n = 4–7 oocytes.

    Techniques Used:

    Docking of BeKm-1 in a model of hERG channel and fluorescent BeKm-1 analogues used in this study. A) Left, BeKm-1 (pdb code: 1j5, magenta, top) in interaction with hERG channel (in solid ribbon representation showing the solvent surface colored by hydrophobicity). The tetrameric model of the hERG channel was generated from the pdb structure (5VA1) using the Prepare Protein module within Discovery Studio. The transmembrane domain, the cytoplasmic N-terminal Per-Arnt-Sim (PAS) domain, the C-terminal C-linker and the cyclic nucleotide binding domain (CNBD) are indicated. Docking of BeKm-1 was performed using the ZDOCK rigid body docking program and refined with the RDOCK module. The top ranked pose of the most populated cluster from the protein-protein interaction predictions is showed with BeKm-1 docked at the top of the transmembrane domain of hERG. Right, Details of the pose of BeKm-1 (magenta) within the interaction surface of hERG colored according to the Solvent Accessibility Surface (SAS) (see Supplementary Data S2), with the side chain of the N terminal Arg 1 and Arg 27 (red) and the more buried C terminal Phe 36 (orange). B) Chemical structures of fluorescent BeKm-1 analogues used in this study with different types of linkers grafted on the N-ter of Arg 1 or the side chain of Arg 27 mutated for a Lysine. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
    Figure Legend Snippet: Docking of BeKm-1 in a model of hERG channel and fluorescent BeKm-1 analogues used in this study. A) Left, BeKm-1 (pdb code: 1j5, magenta, top) in interaction with hERG channel (in solid ribbon representation showing the solvent surface colored by hydrophobicity). The tetrameric model of the hERG channel was generated from the pdb structure (5VA1) using the Prepare Protein module within Discovery Studio. The transmembrane domain, the cytoplasmic N-terminal Per-Arnt-Sim (PAS) domain, the C-terminal C-linker and the cyclic nucleotide binding domain (CNBD) are indicated. Docking of BeKm-1 was performed using the ZDOCK rigid body docking program and refined with the RDOCK module. The top ranked pose of the most populated cluster from the protein-protein interaction predictions is showed with BeKm-1 docked at the top of the transmembrane domain of hERG. Right, Details of the pose of BeKm-1 (magenta) within the interaction surface of hERG colored according to the Solvent Accessibility Surface (SAS) (see Supplementary Data S2), with the side chain of the N terminal Arg 1 and Arg 27 (red) and the more buried C terminal Phe 36 (orange). B) Chemical structures of fluorescent BeKm-1 analogues used in this study with different types of linkers grafted on the N-ter of Arg 1 or the side chain of Arg 27 mutated for a Lysine. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

    Techniques Used: Generated, Binding Assay

    3) Product Images from "Fluorescent analogues of BeKm-1 with high and specific activity against the hERG channel"

    Article Title: Fluorescent analogues of BeKm-1 with high and specific activity against the hERG channel

    Journal: Toxicon: X

    doi: 10.1016/j.toxcx.2019.100010

    The fluorescent BeKm-1 analogues potently inhibit hERG currents. A) Typical traces of currents recorded in Xenopus laevis oocytes that express hERG. Currents were elicited using the protocol depicted at the top in which a pulse from a holding potential of −80 mV to −30 mV precedes a test pulse at −50 mV, in the presence of increasing concentrations of native BeKm-1, Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 or Cy5-PEG5-BeKm1-Lys 27 . Scale bars, 200 nA. B) Inhibition curves of native BeKm-1 and its four analogues. The peak current amplitude was measured during the test pulse at −50 mV in the presence of toxin (ITx) and normalized to the current recorded in the absence of toxin (ICt). Data are the mean ± SEM of n = 4–10 oocytes.
    Figure Legend Snippet: The fluorescent BeKm-1 analogues potently inhibit hERG currents. A) Typical traces of currents recorded in Xenopus laevis oocytes that express hERG. Currents were elicited using the protocol depicted at the top in which a pulse from a holding potential of −80 mV to −30 mV precedes a test pulse at −50 mV, in the presence of increasing concentrations of native BeKm-1, Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 or Cy5-PEG5-BeKm1-Lys 27 . Scale bars, 200 nA. B) Inhibition curves of native BeKm-1 and its four analogues. The peak current amplitude was measured during the test pulse at −50 mV in the presence of toxin (ITx) and normalized to the current recorded in the absence of toxin (ICt). Data are the mean ± SEM of n = 4–10 oocytes.

    Techniques Used: Inhibition

    The mutation S631C in hERG decreases the affinity of native BeKm-1 and of its four fluorescent analogues for the channel. Comparison of the inhibition curves of native BeKm-1 and its four analogues Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 obtained in Xenopus laevis oocytes that express wild type (WT) hERG or the mutant S631C. The data obtained with the mutant channel were fitted by hand for the purpose of comparison. Data are the mean ± SEM of n = 3–5 oocytes.
    Figure Legend Snippet: The mutation S631C in hERG decreases the affinity of native BeKm-1 and of its four fluorescent analogues for the channel. Comparison of the inhibition curves of native BeKm-1 and its four analogues Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 obtained in Xenopus laevis oocytes that express wild type (WT) hERG or the mutant S631C. The data obtained with the mutant channel were fitted by hand for the purpose of comparison. Data are the mean ± SEM of n = 3–5 oocytes.

    Techniques Used: Mutagenesis, Inhibition

    The fluorescent BeKm-1 analogues do not affect hKv10.1 and hKv1.3 currents. A) Typical traces of currents elicited by a step depolarization to 0 mV or 70 mV, from a holding potential of −80 mV, obtained from Xenopus laevis oocytes that express hKv10.1 or hKv1.3, respectively, in the absence or presence of 200 nM native BeKm-1 and in the absence or presence of 500 nM of Cy5-PEG3-linker4-BeKm-1, of Cy5-spacerGS-linker6-BeKm-1, of Cy5-PEG5-linker10-BeKm-1 and of Cy5-PEG5-BeKm1-Lys 27 . Note the lack of effect of BeKm-1 and of the four analogues on both channels. B) Percentage of current remaining in the presence of a single dose of native BeKm-1 or its four analogues (Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 ). Current amplitude was measured before (ICt) and during (Itx) the perfusion of the different toxins. Data are the mean ± SEM of n = 4–7 oocytes.
    Figure Legend Snippet: The fluorescent BeKm-1 analogues do not affect hKv10.1 and hKv1.3 currents. A) Typical traces of currents elicited by a step depolarization to 0 mV or 70 mV, from a holding potential of −80 mV, obtained from Xenopus laevis oocytes that express hKv10.1 or hKv1.3, respectively, in the absence or presence of 200 nM native BeKm-1 and in the absence or presence of 500 nM of Cy5-PEG3-linker4-BeKm-1, of Cy5-spacerGS-linker6-BeKm-1, of Cy5-PEG5-linker10-BeKm-1 and of Cy5-PEG5-BeKm1-Lys 27 . Note the lack of effect of BeKm-1 and of the four analogues on both channels. B) Percentage of current remaining in the presence of a single dose of native BeKm-1 or its four analogues (Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 ). Current amplitude was measured before (ICt) and during (Itx) the perfusion of the different toxins. Data are the mean ± SEM of n = 4–7 oocytes.

    Techniques Used:

    Docking of BeKm-1 in a model of hERG channel and fluorescent BeKm-1 analogues used in this study. A) Left, BeKm-1 (pdb code: 1j5, magenta, top) in interaction with hERG channel (in solid ribbon representation showing the solvent surface colored by hydrophobicity). The tetrameric model of the hERG channel was generated from the pdb structure (5VA1) using the Prepare Protein module within Discovery Studio. The transmembrane domain, the cytoplasmic N-terminal Per-Arnt-Sim (PAS) domain, the C-terminal C-linker and the cyclic nucleotide binding domain (CNBD) are indicated. Docking of BeKm-1 was performed using the ZDOCK rigid body docking program and refined with the RDOCK module. The top ranked pose of the most populated cluster from the protein-protein interaction predictions is showed with BeKm-1 docked at the top of the transmembrane domain of hERG. Right, Details of the pose of BeKm-1 (magenta) within the interaction surface of hERG colored according to the Solvent Accessibility Surface (SAS) (see Supplementary Data S2), with the side chain of the N terminal Arg 1 and Arg 27 (red) and the more buried C terminal Phe 36 (orange). B) Chemical structures of fluorescent BeKm-1 analogues used in this study with different types of linkers grafted on the N-ter of Arg 1 or the side chain of Arg 27 mutated for a Lysine. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
    Figure Legend Snippet: Docking of BeKm-1 in a model of hERG channel and fluorescent BeKm-1 analogues used in this study. A) Left, BeKm-1 (pdb code: 1j5, magenta, top) in interaction with hERG channel (in solid ribbon representation showing the solvent surface colored by hydrophobicity). The tetrameric model of the hERG channel was generated from the pdb structure (5VA1) using the Prepare Protein module within Discovery Studio. The transmembrane domain, the cytoplasmic N-terminal Per-Arnt-Sim (PAS) domain, the C-terminal C-linker and the cyclic nucleotide binding domain (CNBD) are indicated. Docking of BeKm-1 was performed using the ZDOCK rigid body docking program and refined with the RDOCK module. The top ranked pose of the most populated cluster from the protein-protein interaction predictions is showed with BeKm-1 docked at the top of the transmembrane domain of hERG. Right, Details of the pose of BeKm-1 (magenta) within the interaction surface of hERG colored according to the Solvent Accessibility Surface (SAS) (see Supplementary Data S2), with the side chain of the N terminal Arg 1 and Arg 27 (red) and the more buried C terminal Phe 36 (orange). B) Chemical structures of fluorescent BeKm-1 analogues used in this study with different types of linkers grafted on the N-ter of Arg 1 or the side chain of Arg 27 mutated for a Lysine. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

    Techniques Used: Generated, Binding Assay

    4) Product Images from "Fluorescent analogues of BeKm-1 with high and specific activity against the hERG channel"

    Article Title: Fluorescent analogues of BeKm-1 with high and specific activity against the hERG channel

    Journal: Toxicon: X

    doi: 10.1016/j.toxcx.2019.100010

    The fluorescent BeKm-1 analogues potently inhibit hERG currents. A) Typical traces of currents recorded in Xenopus laevis oocytes that express hERG. Currents were elicited using the protocol depicted at the top in which a pulse from a holding potential of −80 mV to −30 mV precedes a test pulse at −50 mV, in the presence of increasing concentrations of native BeKm-1, Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 or Cy5-PEG5-BeKm1-Lys 27 . Scale bars, 200 nA. B) Inhibition curves of native BeKm-1 and its four analogues. The peak current amplitude was measured during the test pulse at −50 mV in the presence of toxin (ITx) and normalized to the current recorded in the absence of toxin (ICt). Data are the mean ± SEM of n = 4–10 oocytes.
    Figure Legend Snippet: The fluorescent BeKm-1 analogues potently inhibit hERG currents. A) Typical traces of currents recorded in Xenopus laevis oocytes that express hERG. Currents were elicited using the protocol depicted at the top in which a pulse from a holding potential of −80 mV to −30 mV precedes a test pulse at −50 mV, in the presence of increasing concentrations of native BeKm-1, Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 or Cy5-PEG5-BeKm1-Lys 27 . Scale bars, 200 nA. B) Inhibition curves of native BeKm-1 and its four analogues. The peak current amplitude was measured during the test pulse at −50 mV in the presence of toxin (ITx) and normalized to the current recorded in the absence of toxin (ICt). Data are the mean ± SEM of n = 4–10 oocytes.

    Techniques Used: Inhibition

    The mutation S631C in hERG decreases the affinity of native BeKm-1 and of its four fluorescent analogues for the channel. Comparison of the inhibition curves of native BeKm-1 and its four analogues Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 obtained in Xenopus laevis oocytes that express wild type (WT) hERG or the mutant S631C. The data obtained with the mutant channel were fitted by hand for the purpose of comparison. Data are the mean ± SEM of n = 3–5 oocytes.
    Figure Legend Snippet: The mutation S631C in hERG decreases the affinity of native BeKm-1 and of its four fluorescent analogues for the channel. Comparison of the inhibition curves of native BeKm-1 and its four analogues Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 obtained in Xenopus laevis oocytes that express wild type (WT) hERG or the mutant S631C. The data obtained with the mutant channel were fitted by hand for the purpose of comparison. Data are the mean ± SEM of n = 3–5 oocytes.

    Techniques Used: Mutagenesis, Inhibition

    The fluorescent BeKm-1 analogues do not affect hKv10.1 and hKv1.3 currents. A) Typical traces of currents elicited by a step depolarization to 0 mV or 70 mV, from a holding potential of −80 mV, obtained from Xenopus laevis oocytes that express hKv10.1 or hKv1.3, respectively, in the absence or presence of 200 nM native BeKm-1 and in the absence or presence of 500 nM of Cy5-PEG3-linker4-BeKm-1, of Cy5-spacerGS-linker6-BeKm-1, of Cy5-PEG5-linker10-BeKm-1 and of Cy5-PEG5-BeKm1-Lys 27 . Note the lack of effect of BeKm-1 and of the four analogues on both channels. B) Percentage of current remaining in the presence of a single dose of native BeKm-1 or its four analogues (Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 ). Current amplitude was measured before (ICt) and during (Itx) the perfusion of the different toxins. Data are the mean ± SEM of n = 4–7 oocytes.
    Figure Legend Snippet: The fluorescent BeKm-1 analogues do not affect hKv10.1 and hKv1.3 currents. A) Typical traces of currents elicited by a step depolarization to 0 mV or 70 mV, from a holding potential of −80 mV, obtained from Xenopus laevis oocytes that express hKv10.1 or hKv1.3, respectively, in the absence or presence of 200 nM native BeKm-1 and in the absence or presence of 500 nM of Cy5-PEG3-linker4-BeKm-1, of Cy5-spacerGS-linker6-BeKm-1, of Cy5-PEG5-linker10-BeKm-1 and of Cy5-PEG5-BeKm1-Lys 27 . Note the lack of effect of BeKm-1 and of the four analogues on both channels. B) Percentage of current remaining in the presence of a single dose of native BeKm-1 or its four analogues (Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 ). Current amplitude was measured before (ICt) and during (Itx) the perfusion of the different toxins. Data are the mean ± SEM of n = 4–7 oocytes.

    Techniques Used:

    Docking of BeKm-1 in a model of hERG channel and fluorescent BeKm-1 analogues used in this study. A) Left, BeKm-1 (pdb code: 1j5, magenta, top) in interaction with hERG channel (in solid ribbon representation showing the solvent surface colored by hydrophobicity). The tetrameric model of the hERG channel was generated from the pdb structure (5VA1) using the Prepare Protein module within Discovery Studio. The transmembrane domain, the cytoplasmic N-terminal Per-Arnt-Sim (PAS) domain, the C-terminal C-linker and the cyclic nucleotide binding domain (CNBD) are indicated. Docking of BeKm-1 was performed using the ZDOCK rigid body docking program and refined with the RDOCK module. The top ranked pose of the most populated cluster from the protein-protein interaction predictions is showed with BeKm-1 docked at the top of the transmembrane domain of hERG. Right, Details of the pose of BeKm-1 (magenta) within the interaction surface of hERG colored according to the Solvent Accessibility Surface (SAS) (see Supplementary Data S2), with the side chain of the N terminal Arg 1 and Arg 27 (red) and the more buried C terminal Phe 36 (orange). B) Chemical structures of fluorescent BeKm-1 analogues used in this study with different types of linkers grafted on the N-ter of Arg 1 or the side chain of Arg 27 mutated for a Lysine. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
    Figure Legend Snippet: Docking of BeKm-1 in a model of hERG channel and fluorescent BeKm-1 analogues used in this study. A) Left, BeKm-1 (pdb code: 1j5, magenta, top) in interaction with hERG channel (in solid ribbon representation showing the solvent surface colored by hydrophobicity). The tetrameric model of the hERG channel was generated from the pdb structure (5VA1) using the Prepare Protein module within Discovery Studio. The transmembrane domain, the cytoplasmic N-terminal Per-Arnt-Sim (PAS) domain, the C-terminal C-linker and the cyclic nucleotide binding domain (CNBD) are indicated. Docking of BeKm-1 was performed using the ZDOCK rigid body docking program and refined with the RDOCK module. The top ranked pose of the most populated cluster from the protein-protein interaction predictions is showed with BeKm-1 docked at the top of the transmembrane domain of hERG. Right, Details of the pose of BeKm-1 (magenta) within the interaction surface of hERG colored according to the Solvent Accessibility Surface (SAS) (see Supplementary Data S2), with the side chain of the N terminal Arg 1 and Arg 27 (red) and the more buried C terminal Phe 36 (orange). B) Chemical structures of fluorescent BeKm-1 analogues used in this study with different types of linkers grafted on the N-ter of Arg 1 or the side chain of Arg 27 mutated for a Lysine. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

    Techniques Used: Generated, Binding Assay

    5) Product Images from "Fluorescent analogues of BeKm-1 with high and specific activity against the hERG channel"

    Article Title: Fluorescent analogues of BeKm-1 with high and specific activity against the hERG channel

    Journal: Toxicon: X

    doi: 10.1016/j.toxcx.2019.100010

    The fluorescent BeKm-1 analogues potently inhibit hERG currents. A) Typical traces of currents recorded in Xenopus laevis oocytes that express hERG. Currents were elicited using the protocol depicted at the top in which a pulse from a holding potential of −80 mV to −30 mV precedes a test pulse at −50 mV, in the presence of increasing concentrations of native BeKm-1, Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 or Cy5-PEG5-BeKm1-Lys 27 . Scale bars, 200 nA. B) Inhibition curves of native BeKm-1 and its four analogues. The peak current amplitude was measured during the test pulse at −50 mV in the presence of toxin (ITx) and normalized to the current recorded in the absence of toxin (ICt). Data are the mean ± SEM of n = 4–10 oocytes.
    Figure Legend Snippet: The fluorescent BeKm-1 analogues potently inhibit hERG currents. A) Typical traces of currents recorded in Xenopus laevis oocytes that express hERG. Currents were elicited using the protocol depicted at the top in which a pulse from a holding potential of −80 mV to −30 mV precedes a test pulse at −50 mV, in the presence of increasing concentrations of native BeKm-1, Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 or Cy5-PEG5-BeKm1-Lys 27 . Scale bars, 200 nA. B) Inhibition curves of native BeKm-1 and its four analogues. The peak current amplitude was measured during the test pulse at −50 mV in the presence of toxin (ITx) and normalized to the current recorded in the absence of toxin (ICt). Data are the mean ± SEM of n = 4–10 oocytes.

    Techniques Used: Inhibition

    The mutation S631C in hERG decreases the affinity of native BeKm-1 and of its four fluorescent analogues for the channel. Comparison of the inhibition curves of native BeKm-1 and its four analogues Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 obtained in Xenopus laevis oocytes that express wild type (WT) hERG or the mutant S631C. The data obtained with the mutant channel were fitted by hand for the purpose of comparison. Data are the mean ± SEM of n = 3–5 oocytes.
    Figure Legend Snippet: The mutation S631C in hERG decreases the affinity of native BeKm-1 and of its four fluorescent analogues for the channel. Comparison of the inhibition curves of native BeKm-1 and its four analogues Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 obtained in Xenopus laevis oocytes that express wild type (WT) hERG or the mutant S631C. The data obtained with the mutant channel were fitted by hand for the purpose of comparison. Data are the mean ± SEM of n = 3–5 oocytes.

    Techniques Used: Mutagenesis, Inhibition

    The fluorescent BeKm-1 analogues do not affect hKv10.1 and hKv1.3 currents. A) Typical traces of currents elicited by a step depolarization to 0 mV or 70 mV, from a holding potential of −80 mV, obtained from Xenopus laevis oocytes that express hKv10.1 or hKv1.3, respectively, in the absence or presence of 200 nM native BeKm-1 and in the absence or presence of 500 nM of Cy5-PEG3-linker4-BeKm-1, of Cy5-spacerGS-linker6-BeKm-1, of Cy5-PEG5-linker10-BeKm-1 and of Cy5-PEG5-BeKm1-Lys 27 . Note the lack of effect of BeKm-1 and of the four analogues on both channels. B) Percentage of current remaining in the presence of a single dose of native BeKm-1 or its four analogues (Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 ). Current amplitude was measured before (ICt) and during (Itx) the perfusion of the different toxins. Data are the mean ± SEM of n = 4–7 oocytes.
    Figure Legend Snippet: The fluorescent BeKm-1 analogues do not affect hKv10.1 and hKv1.3 currents. A) Typical traces of currents elicited by a step depolarization to 0 mV or 70 mV, from a holding potential of −80 mV, obtained from Xenopus laevis oocytes that express hKv10.1 or hKv1.3, respectively, in the absence or presence of 200 nM native BeKm-1 and in the absence or presence of 500 nM of Cy5-PEG3-linker4-BeKm-1, of Cy5-spacerGS-linker6-BeKm-1, of Cy5-PEG5-linker10-BeKm-1 and of Cy5-PEG5-BeKm1-Lys 27 . Note the lack of effect of BeKm-1 and of the four analogues on both channels. B) Percentage of current remaining in the presence of a single dose of native BeKm-1 or its four analogues (Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 ). Current amplitude was measured before (ICt) and during (Itx) the perfusion of the different toxins. Data are the mean ± SEM of n = 4–7 oocytes.

    Techniques Used:

    Docking of BeKm-1 in a model of hERG channel and fluorescent BeKm-1 analogues used in this study. A) Left, BeKm-1 (pdb code: 1j5, magenta, top) in interaction with hERG channel (in solid ribbon representation showing the solvent surface colored by hydrophobicity). The tetrameric model of the hERG channel was generated from the pdb structure (5VA1) using the Prepare Protein module within Discovery Studio. The transmembrane domain, the cytoplasmic N-terminal Per-Arnt-Sim (PAS) domain, the C-terminal C-linker and the cyclic nucleotide binding domain (CNBD) are indicated. Docking of BeKm-1 was performed using the ZDOCK rigid body docking program and refined with the RDOCK module. The top ranked pose of the most populated cluster from the protein-protein interaction predictions is showed with BeKm-1 docked at the top of the transmembrane domain of hERG. Right, Details of the pose of BeKm-1 (magenta) within the interaction surface of hERG colored according to the Solvent Accessibility Surface (SAS) (see Supplementary Data S2), with the side chain of the N terminal Arg 1 and Arg 27 (red) and the more buried C terminal Phe 36 (orange). B) Chemical structures of fluorescent BeKm-1 analogues used in this study with different types of linkers grafted on the N-ter of Arg 1 or the side chain of Arg 27 mutated for a Lysine. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
    Figure Legend Snippet: Docking of BeKm-1 in a model of hERG channel and fluorescent BeKm-1 analogues used in this study. A) Left, BeKm-1 (pdb code: 1j5, magenta, top) in interaction with hERG channel (in solid ribbon representation showing the solvent surface colored by hydrophobicity). The tetrameric model of the hERG channel was generated from the pdb structure (5VA1) using the Prepare Protein module within Discovery Studio. The transmembrane domain, the cytoplasmic N-terminal Per-Arnt-Sim (PAS) domain, the C-terminal C-linker and the cyclic nucleotide binding domain (CNBD) are indicated. Docking of BeKm-1 was performed using the ZDOCK rigid body docking program and refined with the RDOCK module. The top ranked pose of the most populated cluster from the protein-protein interaction predictions is showed with BeKm-1 docked at the top of the transmembrane domain of hERG. Right, Details of the pose of BeKm-1 (magenta) within the interaction surface of hERG colored according to the Solvent Accessibility Surface (SAS) (see Supplementary Data S2), with the side chain of the N terminal Arg 1 and Arg 27 (red) and the more buried C terminal Phe 36 (orange). B) Chemical structures of fluorescent BeKm-1 analogues used in this study with different types of linkers grafted on the N-ter of Arg 1 or the side chain of Arg 27 mutated for a Lysine. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

    Techniques Used: Generated, Binding Assay

    6) Product Images from "Fluorescent analogues of BeKm-1 with high and specific activity against the hERG channel"

    Article Title: Fluorescent analogues of BeKm-1 with high and specific activity against the hERG channel

    Journal: Toxicon: X

    doi: 10.1016/j.toxcx.2019.100010

    The fluorescent BeKm-1 analogues potently inhibit hERG currents. A) Typical traces of currents recorded in Xenopus laevis oocytes that express hERG. Currents were elicited using the protocol depicted at the top in which a pulse from a holding potential of −80 mV to −30 mV precedes a test pulse at −50 mV, in the presence of increasing concentrations of native BeKm-1, Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 or Cy5-PEG5-BeKm1-Lys 27 . Scale bars, 200 nA. B) Inhibition curves of native BeKm-1 and its four analogues. The peak current amplitude was measured during the test pulse at −50 mV in the presence of toxin (ITx) and normalized to the current recorded in the absence of toxin (ICt). Data are the mean ± SEM of n = 4–10 oocytes.
    Figure Legend Snippet: The fluorescent BeKm-1 analogues potently inhibit hERG currents. A) Typical traces of currents recorded in Xenopus laevis oocytes that express hERG. Currents were elicited using the protocol depicted at the top in which a pulse from a holding potential of −80 mV to −30 mV precedes a test pulse at −50 mV, in the presence of increasing concentrations of native BeKm-1, Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 or Cy5-PEG5-BeKm1-Lys 27 . Scale bars, 200 nA. B) Inhibition curves of native BeKm-1 and its four analogues. The peak current amplitude was measured during the test pulse at −50 mV in the presence of toxin (ITx) and normalized to the current recorded in the absence of toxin (ICt). Data are the mean ± SEM of n = 4–10 oocytes.

    Techniques Used: Inhibition

    The mutation S631C in hERG decreases the affinity of native BeKm-1 and of its four fluorescent analogues for the channel. Comparison of the inhibition curves of native BeKm-1 and its four analogues Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 obtained in Xenopus laevis oocytes that express wild type (WT) hERG or the mutant S631C. The data obtained with the mutant channel were fitted by hand for the purpose of comparison. Data are the mean ± SEM of n = 3–5 oocytes.
    Figure Legend Snippet: The mutation S631C in hERG decreases the affinity of native BeKm-1 and of its four fluorescent analogues for the channel. Comparison of the inhibition curves of native BeKm-1 and its four analogues Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 obtained in Xenopus laevis oocytes that express wild type (WT) hERG or the mutant S631C. The data obtained with the mutant channel were fitted by hand for the purpose of comparison. Data are the mean ± SEM of n = 3–5 oocytes.

    Techniques Used: Mutagenesis, Inhibition

    The fluorescent BeKm-1 analogues do not affect hKv10.1 and hKv1.3 currents. A) Typical traces of currents elicited by a step depolarization to 0 mV or 70 mV, from a holding potential of −80 mV, obtained from Xenopus laevis oocytes that express hKv10.1 or hKv1.3, respectively, in the absence or presence of 200 nM native BeKm-1 and in the absence or presence of 500 nM of Cy5-PEG3-linker4-BeKm-1, of Cy5-spacerGS-linker6-BeKm-1, of Cy5-PEG5-linker10-BeKm-1 and of Cy5-PEG5-BeKm1-Lys 27 . Note the lack of effect of BeKm-1 and of the four analogues on both channels. B) Percentage of current remaining in the presence of a single dose of native BeKm-1 or its four analogues (Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 ). Current amplitude was measured before (ICt) and during (Itx) the perfusion of the different toxins. Data are the mean ± SEM of n = 4–7 oocytes.
    Figure Legend Snippet: The fluorescent BeKm-1 analogues do not affect hKv10.1 and hKv1.3 currents. A) Typical traces of currents elicited by a step depolarization to 0 mV or 70 mV, from a holding potential of −80 mV, obtained from Xenopus laevis oocytes that express hKv10.1 or hKv1.3, respectively, in the absence or presence of 200 nM native BeKm-1 and in the absence or presence of 500 nM of Cy5-PEG3-linker4-BeKm-1, of Cy5-spacerGS-linker6-BeKm-1, of Cy5-PEG5-linker10-BeKm-1 and of Cy5-PEG5-BeKm1-Lys 27 . Note the lack of effect of BeKm-1 and of the four analogues on both channels. B) Percentage of current remaining in the presence of a single dose of native BeKm-1 or its four analogues (Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 ). Current amplitude was measured before (ICt) and during (Itx) the perfusion of the different toxins. Data are the mean ± SEM of n = 4–7 oocytes.

    Techniques Used:

    Docking of BeKm-1 in a model of hERG channel and fluorescent BeKm-1 analogues used in this study. A) Left, BeKm-1 (pdb code: 1j5, magenta, top) in interaction with hERG channel (in solid ribbon representation showing the solvent surface colored by hydrophobicity). The tetrameric model of the hERG channel was generated from the pdb structure (5VA1) using the Prepare Protein module within Discovery Studio. The transmembrane domain, the cytoplasmic N-terminal Per-Arnt-Sim (PAS) domain, the C-terminal C-linker and the cyclic nucleotide binding domain (CNBD) are indicated. Docking of BeKm-1 was performed using the ZDOCK rigid body docking program and refined with the RDOCK module. The top ranked pose of the most populated cluster from the protein-protein interaction predictions is showed with BeKm-1 docked at the top of the transmembrane domain of hERG. Right, Details of the pose of BeKm-1 (magenta) within the interaction surface of hERG colored according to the Solvent Accessibility Surface (SAS) (see Supplementary Data S2), with the side chain of the N terminal Arg 1 and Arg 27 (red) and the more buried C terminal Phe 36 (orange). B) Chemical structures of fluorescent BeKm-1 analogues used in this study with different types of linkers grafted on the N-ter of Arg 1 or the side chain of Arg 27 mutated for a Lysine. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
    Figure Legend Snippet: Docking of BeKm-1 in a model of hERG channel and fluorescent BeKm-1 analogues used in this study. A) Left, BeKm-1 (pdb code: 1j5, magenta, top) in interaction with hERG channel (in solid ribbon representation showing the solvent surface colored by hydrophobicity). The tetrameric model of the hERG channel was generated from the pdb structure (5VA1) using the Prepare Protein module within Discovery Studio. The transmembrane domain, the cytoplasmic N-terminal Per-Arnt-Sim (PAS) domain, the C-terminal C-linker and the cyclic nucleotide binding domain (CNBD) are indicated. Docking of BeKm-1 was performed using the ZDOCK rigid body docking program and refined with the RDOCK module. The top ranked pose of the most populated cluster from the protein-protein interaction predictions is showed with BeKm-1 docked at the top of the transmembrane domain of hERG. Right, Details of the pose of BeKm-1 (magenta) within the interaction surface of hERG colored according to the Solvent Accessibility Surface (SAS) (see Supplementary Data S2), with the side chain of the N terminal Arg 1 and Arg 27 (red) and the more buried C terminal Phe 36 (orange). B) Chemical structures of fluorescent BeKm-1 analogues used in this study with different types of linkers grafted on the N-ter of Arg 1 or the side chain of Arg 27 mutated for a Lysine. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

    Techniques Used: Generated, Binding Assay

    7) Product Images from "Transfer of Rolf S3-S4 Linker to hERG Eliminates Activation Gating but Spares Inactivation"

    Article Title: Transfer of Rolf S3-S4 Linker to hERG Eliminates Activation Gating but Spares Inactivation

    Journal:

    doi: 10.1016/j.bpj.2009.05.060

    Effect of BeKm-1 on hERG and the chimera. Representative currents of ( A ) hERG and the ( B ) chimera in baseline conditions and after a 3-min exposure to 25 nM BeKm-1 elicited by an ascending voltage ramp (10 mV/s; every 15 s). ( C ) Mean fractional block
    Figure Legend Snippet: Effect of BeKm-1 on hERG and the chimera. Representative currents of ( A ) hERG and the ( B ) chimera in baseline conditions and after a 3-min exposure to 25 nM BeKm-1 elicited by an ascending voltage ramp (10 mV/s; every 15 s). ( C ) Mean fractional block

    Techniques Used: Blocking Assay

    8) Product Images from "Probing the Binding Sites and Mechanisms of Action of Two Human Ether-a-go-go-Related Gene Channel Activators, 1,3-bis-(2-Hydroxy-5-trifluoromethyl-phenyl)-urea (NS1643) and 2-[2-(3,4-Dichloro-phenyl)-2,3-dihydro-1H-isoindol-5-ylamino]-nicotinic acid (PD307243)"

    Article Title: Probing the Binding Sites and Mechanisms of Action of Two Human Ether-a-go-go-Related Gene Channel Activators, 1,3-bis-(2-Hydroxy-5-trifluoromethyl-phenyl)-urea (NS1643) and 2-[2-(3,4-Dichloro-phenyl)-2,3-dihydro-1H-isoindol-5-ylamino]-nicotinic acid (PD307243)

    Journal:

    doi: 10.1124/mol.108.045591

    BeKm-1 potentiated the activator effect of PD307243 but suppressed the activator effect of NS1643. A, cartoon of hERG pore domain with an extracellular BeKm-1 structure. Three hERG subunits are depicted, with the fourth one closest to viewers removed
    Figure Legend Snippet: BeKm-1 potentiated the activator effect of PD307243 but suppressed the activator effect of NS1643. A, cartoon of hERG pore domain with an extracellular BeKm-1 structure. Three hERG subunits are depicted, with the fourth one closest to viewers removed

    Techniques Used:

    9) Product Images from "Probing the Binding Sites and Mechanisms of Action of Two Human Ether-a-go-go-Related Gene Channel Activators, 1,3-bis-(2-Hydroxy-5-trifluoromethyl-phenyl)-urea (NS1643) and 2-[2-(3,4-Dichloro-phenyl)-2,3-dihydro-1H-isoindol-5-ylamino]-nicotinic acid (PD307243) s"

    Article Title: Probing the Binding Sites and Mechanisms of Action of Two Human Ether-a-go-go-Related Gene Channel Activators, 1,3-bis-(2-Hydroxy-5-trifluoromethyl-phenyl)-urea (NS1643) and 2-[2-(3,4-Dichloro-phenyl)-2,3-dihydro-1H-isoindol-5-ylamino]-nicotinic acid (PD307243) s

    Journal:

    doi: 10.1124/mol.108.045591

    BeKm-1 potentiated the activator effect of PD307243 but suppressed the activator effect of NS1643. A, cartoon of hERG pore domain with an extracellular BeKm-1 structure. Three hERG subunits are depicted, with the fourth one closest to viewers removed
    Figure Legend Snippet: BeKm-1 potentiated the activator effect of PD307243 but suppressed the activator effect of NS1643. A, cartoon of hERG pore domain with an extracellular BeKm-1 structure. Three hERG subunits are depicted, with the fourth one closest to viewers removed

    Techniques Used:

    10) Product Images from "Probing the Binding Sites and Mechanisms of Action of Two Human Ether-a-go-go-Related Gene Channel Activators, 1,3-bis-(2-Hydroxy-5-trifluoromethyl-phenyl)-urea (NS1643) and 2-[2-(3,4-Dichloro-phenyl)-2,3-dihydro-1H-isoindol-5-ylamino]-nicotinic acid (PD307243) s"

    Article Title: Probing the Binding Sites and Mechanisms of Action of Two Human Ether-a-go-go-Related Gene Channel Activators, 1,3-bis-(2-Hydroxy-5-trifluoromethyl-phenyl)-urea (NS1643) and 2-[2-(3,4-Dichloro-phenyl)-2,3-dihydro-1H-isoindol-5-ylamino]-nicotinic acid (PD307243) s

    Journal:

    doi: 10.1124/mol.108.045591

    BeKm-1 potentiated the activator effect of PD307243 but suppressed the activator effect of NS1643. A, cartoon of hERG pore domain with an extracellular BeKm-1 structure. Three hERG subunits are depicted, with the fourth one closest to viewers removed
    Figure Legend Snippet: BeKm-1 potentiated the activator effect of PD307243 but suppressed the activator effect of NS1643. A, cartoon of hERG pore domain with an extracellular BeKm-1 structure. Three hERG subunits are depicted, with the fourth one closest to viewers removed

    Techniques Used:

    11) Product Images from "Probing the Binding Sites and Mechanisms of Action of Two Human Ether-a-go-go-Related Gene Channel Activators, 1,3-bis-(2-Hydroxy-5-trifluoromethyl-phenyl)-urea (NS1643) and 2-[2-(3,4-Dichloro-phenyl)-2,3-dihydro-1H-isoindol-5-ylamino]-nicotinic acid (PD307243) s"

    Article Title: Probing the Binding Sites and Mechanisms of Action of Two Human Ether-a-go-go-Related Gene Channel Activators, 1,3-bis-(2-Hydroxy-5-trifluoromethyl-phenyl)-urea (NS1643) and 2-[2-(3,4-Dichloro-phenyl)-2,3-dihydro-1H-isoindol-5-ylamino]-nicotinic acid (PD307243) s

    Journal:

    doi: 10.1124/mol.108.045591

    BeKm-1 potentiated the activator effect of PD307243 but suppressed the activator effect of NS1643. A, cartoon of hERG pore domain with an extracellular BeKm-1 structure. Three hERG subunits are depicted, with the fourth one closest to viewers removed
    Figure Legend Snippet: BeKm-1 potentiated the activator effect of PD307243 but suppressed the activator effect of NS1643. A, cartoon of hERG pore domain with an extracellular BeKm-1 structure. Three hERG subunits are depicted, with the fourth one closest to viewers removed

    Techniques Used:

    12) Product Images from "Probing the Binding Sites and Mechanisms of Action of Two Human Ether-a-go-go-Related Gene Channel Activators, 1,3-bis-(2-Hydroxy-5-trifluoromethyl-phenyl)-urea (NS1643) and 2-[2-(3,4-Dichloro-phenyl)-2,3-dihydro-1H-isoindol-5-ylamino]-nicotinic acid (PD307243) s"

    Article Title: Probing the Binding Sites and Mechanisms of Action of Two Human Ether-a-go-go-Related Gene Channel Activators, 1,3-bis-(2-Hydroxy-5-trifluoromethyl-phenyl)-urea (NS1643) and 2-[2-(3,4-Dichloro-phenyl)-2,3-dihydro-1H-isoindol-5-ylamino]-nicotinic acid (PD307243) s

    Journal:

    doi: 10.1124/mol.108.045591

    BeKm-1 potentiated the activator effect of PD307243 but suppressed the activator effect of NS1643. A, cartoon of hERG pore domain with an extracellular BeKm-1 structure. Three hERG subunits are depicted, with the fourth one closest to viewers removed
    Figure Legend Snippet: BeKm-1 potentiated the activator effect of PD307243 but suppressed the activator effect of NS1643. A, cartoon of hERG pore domain with an extracellular BeKm-1 structure. Three hERG subunits are depicted, with the fourth one closest to viewers removed

    Techniques Used:

    13) Product Images from "Probing the Binding Sites and Mechanisms of Action of Two Human Ether-a-go-go-Related Gene Channel Activators, 1,3-bis-(2-Hydroxy-5-trifluoromethyl-phenyl)-urea (NS1643) and 2-[2-(3,4-Dichloro-phenyl)-2,3-dihydro-1H-isoindol-5-ylamino]-nicotinic acid (PD307243) s"

    Article Title: Probing the Binding Sites and Mechanisms of Action of Two Human Ether-a-go-go-Related Gene Channel Activators, 1,3-bis-(2-Hydroxy-5-trifluoromethyl-phenyl)-urea (NS1643) and 2-[2-(3,4-Dichloro-phenyl)-2,3-dihydro-1H-isoindol-5-ylamino]-nicotinic acid (PD307243) s

    Journal:

    doi: 10.1124/mol.108.045591

    BeKm-1 potentiated the activator effect of PD307243 but suppressed the activator effect of NS1643. A, cartoon of hERG pore domain with an extracellular BeKm-1 structure. Three hERG subunits are depicted, with the fourth one closest to viewers removed
    Figure Legend Snippet: BeKm-1 potentiated the activator effect of PD307243 but suppressed the activator effect of NS1643. A, cartoon of hERG pore domain with an extracellular BeKm-1 structure. Three hERG subunits are depicted, with the fourth one closest to viewers removed

    Techniques Used:

    14) Product Images from "Probing the Binding Sites and Mechanisms of Action of Two Human Ether-a-go-go-Related Gene Channel Activators, 1,3-bis-(2-Hydroxy-5-trifluoromethyl-phenyl)-urea (NS1643) and 2-[2-(3,4-Dichloro-phenyl)-2,3-dihydro-1H-isoindol-5-ylamino]-nicotinic acid (PD307243) s"

    Article Title: Probing the Binding Sites and Mechanisms of Action of Two Human Ether-a-go-go-Related Gene Channel Activators, 1,3-bis-(2-Hydroxy-5-trifluoromethyl-phenyl)-urea (NS1643) and 2-[2-(3,4-Dichloro-phenyl)-2,3-dihydro-1H-isoindol-5-ylamino]-nicotinic acid (PD307243) s

    Journal:

    doi: 10.1124/mol.108.045591

    BeKm-1 potentiated the activator effect of PD307243 but suppressed the activator effect of NS1643. A, cartoon of hERG pore domain with an extracellular BeKm-1 structure. Three hERG subunits are depicted, with the fourth one closest to viewers removed
    Figure Legend Snippet: BeKm-1 potentiated the activator effect of PD307243 but suppressed the activator effect of NS1643. A, cartoon of hERG pore domain with an extracellular BeKm-1 structure. Three hERG subunits are depicted, with the fourth one closest to viewers removed

    Techniques Used:

    15) Product Images from "Probing the Binding Sites and Mechanisms of Action of Two Human Ether-a-go-go-Related Gene Channel Activators, 1,3-bis-(2-Hydroxy-5-trifluoromethyl-phenyl)-urea (NS1643) and 2-[2-(3,4-Dichloro-phenyl)-2,3-dihydro-1H-isoindol-5-ylamino]-nicotinic acid (PD307243) s"

    Article Title: Probing the Binding Sites and Mechanisms of Action of Two Human Ether-a-go-go-Related Gene Channel Activators, 1,3-bis-(2-Hydroxy-5-trifluoromethyl-phenyl)-urea (NS1643) and 2-[2-(3,4-Dichloro-phenyl)-2,3-dihydro-1H-isoindol-5-ylamino]-nicotinic acid (PD307243) s

    Journal:

    doi: 10.1124/mol.108.045591

    BeKm-1 potentiated the activator effect of PD307243 but suppressed the activator effect of NS1643. A, cartoon of hERG pore domain with an extracellular BeKm-1 structure. Three hERG subunits are depicted, with the fourth one closest to viewers removed
    Figure Legend Snippet: BeKm-1 potentiated the activator effect of PD307243 but suppressed the activator effect of NS1643. A, cartoon of hERG pore domain with an extracellular BeKm-1 structure. Three hERG subunits are depicted, with the fourth one closest to viewers removed

    Techniques Used:

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    Alomone Labs recombinant toxin bekm 1
    The fluorescent <t>BeKm-1</t> analogues potently inhibit hERG currents. A) Typical traces of currents recorded in Xenopus laevis oocytes that express hERG. Currents were elicited using the protocol depicted at the top in which a pulse from a holding potential of −80 mV to −30 mV precedes a test pulse at −50 mV, in the presence of increasing concentrations of native BeKm-1, Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 or Cy5-PEG5-BeKm1-Lys 27 . Scale bars, 200 nA. B) Inhibition curves of native BeKm-1 and its four analogues. The peak current amplitude was measured during the test pulse at −50 mV in the presence of toxin (ITx) and normalized to the current recorded in the absence of toxin (ICt). Data are the mean ± SEM of n = 4–10 oocytes.
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    The fluorescent BeKm-1 analogues potently inhibit hERG currents. A) Typical traces of currents recorded in Xenopus laevis oocytes that express hERG. Currents were elicited using the protocol depicted at the top in which a pulse from a holding potential of −80 mV to −30 mV precedes a test pulse at −50 mV, in the presence of increasing concentrations of native BeKm-1, Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 or Cy5-PEG5-BeKm1-Lys 27 . Scale bars, 200 nA. B) Inhibition curves of native BeKm-1 and its four analogues. The peak current amplitude was measured during the test pulse at −50 mV in the presence of toxin (ITx) and normalized to the current recorded in the absence of toxin (ICt). Data are the mean ± SEM of n = 4–10 oocytes.

    Journal: Toxicon: X

    Article Title: Fluorescent analogues of BeKm-1 with high and specific activity against the hERG channel

    doi: 10.1016/j.toxcx.2019.100010

    Figure Lengend Snippet: The fluorescent BeKm-1 analogues potently inhibit hERG currents. A) Typical traces of currents recorded in Xenopus laevis oocytes that express hERG. Currents were elicited using the protocol depicted at the top in which a pulse from a holding potential of −80 mV to −30 mV precedes a test pulse at −50 mV, in the presence of increasing concentrations of native BeKm-1, Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 or Cy5-PEG5-BeKm1-Lys 27 . Scale bars, 200 nA. B) Inhibition curves of native BeKm-1 and its four analogues. The peak current amplitude was measured during the test pulse at −50 mV in the presence of toxin (ITx) and normalized to the current recorded in the absence of toxin (ICt). Data are the mean ± SEM of n = 4–10 oocytes.

    Article Snippet: 3.4 Effects of native BeKm-1 and its analogues on the hKv 10.1 and Kv 1.3 currents We then checked whether labeling affected BeKm-1 specificity or whether the grafted chemical groups induce any block of K+ channels insensitive to the BeKm-1 toxin.

    Techniques: Inhibition

    The mutation S631C in hERG decreases the affinity of native BeKm-1 and of its four fluorescent analogues for the channel. Comparison of the inhibition curves of native BeKm-1 and its four analogues Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 obtained in Xenopus laevis oocytes that express wild type (WT) hERG or the mutant S631C. The data obtained with the mutant channel were fitted by hand for the purpose of comparison. Data are the mean ± SEM of n = 3–5 oocytes.

    Journal: Toxicon: X

    Article Title: Fluorescent analogues of BeKm-1 with high and specific activity against the hERG channel

    doi: 10.1016/j.toxcx.2019.100010

    Figure Lengend Snippet: The mutation S631C in hERG decreases the affinity of native BeKm-1 and of its four fluorescent analogues for the channel. Comparison of the inhibition curves of native BeKm-1 and its four analogues Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 obtained in Xenopus laevis oocytes that express wild type (WT) hERG or the mutant S631C. The data obtained with the mutant channel were fitted by hand for the purpose of comparison. Data are the mean ± SEM of n = 3–5 oocytes.

    Article Snippet: 3.4 Effects of native BeKm-1 and its analogues on the hKv 10.1 and Kv 1.3 currents We then checked whether labeling affected BeKm-1 specificity or whether the grafted chemical groups induce any block of K+ channels insensitive to the BeKm-1 toxin.

    Techniques: Mutagenesis, Inhibition

    The fluorescent BeKm-1 analogues do not affect hKv10.1 and hKv1.3 currents. A) Typical traces of currents elicited by a step depolarization to 0 mV or 70 mV, from a holding potential of −80 mV, obtained from Xenopus laevis oocytes that express hKv10.1 or hKv1.3, respectively, in the absence or presence of 200 nM native BeKm-1 and in the absence or presence of 500 nM of Cy5-PEG3-linker4-BeKm-1, of Cy5-spacerGS-linker6-BeKm-1, of Cy5-PEG5-linker10-BeKm-1 and of Cy5-PEG5-BeKm1-Lys 27 . Note the lack of effect of BeKm-1 and of the four analogues on both channels. B) Percentage of current remaining in the presence of a single dose of native BeKm-1 or its four analogues (Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 ). Current amplitude was measured before (ICt) and during (Itx) the perfusion of the different toxins. Data are the mean ± SEM of n = 4–7 oocytes.

    Journal: Toxicon: X

    Article Title: Fluorescent analogues of BeKm-1 with high and specific activity against the hERG channel

    doi: 10.1016/j.toxcx.2019.100010

    Figure Lengend Snippet: The fluorescent BeKm-1 analogues do not affect hKv10.1 and hKv1.3 currents. A) Typical traces of currents elicited by a step depolarization to 0 mV or 70 mV, from a holding potential of −80 mV, obtained from Xenopus laevis oocytes that express hKv10.1 or hKv1.3, respectively, in the absence or presence of 200 nM native BeKm-1 and in the absence or presence of 500 nM of Cy5-PEG3-linker4-BeKm-1, of Cy5-spacerGS-linker6-BeKm-1, of Cy5-PEG5-linker10-BeKm-1 and of Cy5-PEG5-BeKm1-Lys 27 . Note the lack of effect of BeKm-1 and of the four analogues on both channels. B) Percentage of current remaining in the presence of a single dose of native BeKm-1 or its four analogues (Cy5-PEG3-linker4-BeKm-1, Cy5-spacerGS-linker6-BeKm-1, Cy5-PEG5-linker10-BeKm-1 and Cy5-PEG5-BeKm1-Lys 27 ). Current amplitude was measured before (ICt) and during (Itx) the perfusion of the different toxins. Data are the mean ± SEM of n = 4–7 oocytes.

    Article Snippet: 3.4 Effects of native BeKm-1 and its analogues on the hKv 10.1 and Kv 1.3 currents We then checked whether labeling affected BeKm-1 specificity or whether the grafted chemical groups induce any block of K+ channels insensitive to the BeKm-1 toxin.

    Techniques:

    Docking of BeKm-1 in a model of hERG channel and fluorescent BeKm-1 analogues used in this study. A) Left, BeKm-1 (pdb code: 1j5, magenta, top) in interaction with hERG channel (in solid ribbon representation showing the solvent surface colored by hydrophobicity). The tetrameric model of the hERG channel was generated from the pdb structure (5VA1) using the Prepare Protein module within Discovery Studio. The transmembrane domain, the cytoplasmic N-terminal Per-Arnt-Sim (PAS) domain, the C-terminal C-linker and the cyclic nucleotide binding domain (CNBD) are indicated. Docking of BeKm-1 was performed using the ZDOCK rigid body docking program and refined with the RDOCK module. The top ranked pose of the most populated cluster from the protein-protein interaction predictions is showed with BeKm-1 docked at the top of the transmembrane domain of hERG. Right, Details of the pose of BeKm-1 (magenta) within the interaction surface of hERG colored according to the Solvent Accessibility Surface (SAS) (see Supplementary Data S2), with the side chain of the N terminal Arg 1 and Arg 27 (red) and the more buried C terminal Phe 36 (orange). B) Chemical structures of fluorescent BeKm-1 analogues used in this study with different types of linkers grafted on the N-ter of Arg 1 or the side chain of Arg 27 mutated for a Lysine. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

    Journal: Toxicon: X

    Article Title: Fluorescent analogues of BeKm-1 with high and specific activity against the hERG channel

    doi: 10.1016/j.toxcx.2019.100010

    Figure Lengend Snippet: Docking of BeKm-1 in a model of hERG channel and fluorescent BeKm-1 analogues used in this study. A) Left, BeKm-1 (pdb code: 1j5, magenta, top) in interaction with hERG channel (in solid ribbon representation showing the solvent surface colored by hydrophobicity). The tetrameric model of the hERG channel was generated from the pdb structure (5VA1) using the Prepare Protein module within Discovery Studio. The transmembrane domain, the cytoplasmic N-terminal Per-Arnt-Sim (PAS) domain, the C-terminal C-linker and the cyclic nucleotide binding domain (CNBD) are indicated. Docking of BeKm-1 was performed using the ZDOCK rigid body docking program and refined with the RDOCK module. The top ranked pose of the most populated cluster from the protein-protein interaction predictions is showed with BeKm-1 docked at the top of the transmembrane domain of hERG. Right, Details of the pose of BeKm-1 (magenta) within the interaction surface of hERG colored according to the Solvent Accessibility Surface (SAS) (see Supplementary Data S2), with the side chain of the N terminal Arg 1 and Arg 27 (red) and the more buried C terminal Phe 36 (orange). B) Chemical structures of fluorescent BeKm-1 analogues used in this study with different types of linkers grafted on the N-ter of Arg 1 or the side chain of Arg 27 mutated for a Lysine. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

    Article Snippet: 3.4 Effects of native BeKm-1 and its analogues on the hKv 10.1 and Kv 1.3 currents We then checked whether labeling affected BeKm-1 specificity or whether the grafted chemical groups induce any block of K+ channels insensitive to the BeKm-1 toxin.

    Techniques: Generated, Binding Assay