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  • 99
    Millipore peptide synthesis peptides
    <t>CMA3</t> peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4
    Peptide Synthesis Peptides, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 172 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher peptides synthesizer
    <t>CMA3</t> peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4
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    CEM Corporation peptides synthesizer
    <t>CMA3</t> peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4
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    ProteoGenix peptides synthesis nc1 xix peptide
    <t>CMA3</t> peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4
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    INTAVIS peptide synthesis peptides
    <t>CMA3</t> peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4
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    CEM Corporation peptide synthesis peptides
    <t>CMA3</t> peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4
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    SPSS Inc peptide synthesis peptides
    <t>CMA3</t> peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4
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    GenScript peptide synthesis peptides
    <t>CMA3</t> peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4
    Peptide Synthesis Peptides, supplied by GenScript, used in various techniques. Bioz Stars score: 92/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    CS Bio peptide synthesis peptides
    <t>CMA3</t> peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4
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    Peptron Inc peptide synthesis peptides
    <t>CMA3</t> peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4
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    AAPPTec peptide synthesis peptides
    <t>CMA3</t> peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4
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    BIOTAGE peptide synthesis peptides
    <t>CMA3</t> peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4
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    Sigma-Genosys peptide synthesis peptides
    <t>CMA3</t> peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4
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    Bio-Synthesis Inc peptide synthesis peptides
    <t>CMA3</t> peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4
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    Mimotopes peptide synthesis peptides
    <t>CMA3</t> peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4
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    AnaSpec peptide synthesis peptides
    <t>CMA3</t> peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4
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    GL Biochem peptide synthesis peptides
    <t>CMA3</t> peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4
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    WuXi AppTec peptide synthesis peptides
    <t>CMA3</t> peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4
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    Proteintech peptide synthesis peptides
    <t>CMA3</t> peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4
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    Image Search Results


    CMA3 peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4

    Journal: Nanoscale Research Letters

    Article Title: A Protein Nanopore-Based Approach for Bacteria Sensing

    doi: 10.1186/s11671-016-1715-z

    Figure Lengend Snippet: CMA3 peptide influence on the voltage dependence of P.a. capture by the α-HL nanopore at acidic pH. Data points represent rate on values versus Δ V measured in the absence ( open triangles ) and presence of 20 μM CMA3 peptide ( full triangles ), at pH = 4

    Article Snippet: CMA3 Peptide Synthesis and Purification The CMA3 peptide (KWKLKKHIGIGKHFLSAKKF-NH2) was synthesized as previously described [ ] using the 9-fluorenylmethoxycarbonyl (Fmoc) solid-phase method on Rink amide 4-methyl benzhydrylamine resin (0.55 mmol/g; Novabiochem, Darmstadt, Germany) with a Liberty microwave peptide synthesizer (CEM Co., Matthews, NC, USA).

    Techniques:

    Electrical characterization of P. aeruginosa ( P.a. ) interaction with the α-HL at acidic pH. Comparison of P.a. -induced ion current blockades through the α-HL recorded at pH = 4 and Δ V = −70 mV, in the absence ( a ) and presence of the trans -added CMA3 peptide ( b ). In c and d , we show the events scatter plots of Δ I block and dwell times of the free and P.a. -blocked α-HL corresponding to the representative traces shown in a and b . The comparison of dwell times distribution corresponding to the “free pore” reveals the virtual absence of the CMA3 peptide effect on bacterial cells association to the nanopore

    Journal: Nanoscale Research Letters

    Article Title: A Protein Nanopore-Based Approach for Bacteria Sensing

    doi: 10.1186/s11671-016-1715-z

    Figure Lengend Snippet: Electrical characterization of P. aeruginosa ( P.a. ) interaction with the α-HL at acidic pH. Comparison of P.a. -induced ion current blockades through the α-HL recorded at pH = 4 and Δ V = −70 mV, in the absence ( a ) and presence of the trans -added CMA3 peptide ( b ). In c and d , we show the events scatter plots of Δ I block and dwell times of the free and P.a. -blocked α-HL corresponding to the representative traces shown in a and b . The comparison of dwell times distribution corresponding to the “free pore” reveals the virtual absence of the CMA3 peptide effect on bacterial cells association to the nanopore

    Article Snippet: CMA3 Peptide Synthesis and Purification The CMA3 peptide (KWKLKKHIGIGKHFLSAKKF-NH2) was synthesized as previously described [ ] using the 9-fluorenylmethoxycarbonyl (Fmoc) solid-phase method on Rink amide 4-methyl benzhydrylamine resin (0.55 mmol/g; Novabiochem, Darmstadt, Germany) with a Liberty microwave peptide synthesizer (CEM Co., Matthews, NC, USA).

    Techniques: Blocking Assay

    Cartoon representation (not drawn to the scale) reflecting the putative role played by the CMA3 peptide adsorption to P.a. , on the bacterial cell capture process. As compared to the control case (no peptide, a ), the cationic CMA3 peptide (charge = + 8| e − | at pH = 7) adsorption to P.a. ( b ) determines a net decrease on the bacterial surface charge on the outer membrane (Q), at pH = 7. The charge reduction on bacterial surface leads to an augmented association rate of the P.a. -α-HL interactions, resulting from the reduced magnitude of electrostatic repulsive forces manifested between the negatively charged bacteria and the lumen entrance of the α-HL (F p-b ), which over-compensates for the reduced electrophoretic force ( F elp ) acting on the bacterium (see text). Around neutral pH, the net electric charge present at the entrance of α-HL’s lumen is ~ − 7| e − |

    Journal: Nanoscale Research Letters

    Article Title: A Protein Nanopore-Based Approach for Bacteria Sensing

    doi: 10.1186/s11671-016-1715-z

    Figure Lengend Snippet: Cartoon representation (not drawn to the scale) reflecting the putative role played by the CMA3 peptide adsorption to P.a. , on the bacterial cell capture process. As compared to the control case (no peptide, a ), the cationic CMA3 peptide (charge = + 8| e − | at pH = 7) adsorption to P.a. ( b ) determines a net decrease on the bacterial surface charge on the outer membrane (Q), at pH = 7. The charge reduction on bacterial surface leads to an augmented association rate of the P.a. -α-HL interactions, resulting from the reduced magnitude of electrostatic repulsive forces manifested between the negatively charged bacteria and the lumen entrance of the α-HL (F p-b ), which over-compensates for the reduced electrophoretic force ( F elp ) acting on the bacterium (see text). Around neutral pH, the net electric charge present at the entrance of α-HL’s lumen is ~ − 7| e − |

    Article Snippet: CMA3 Peptide Synthesis and Purification The CMA3 peptide (KWKLKKHIGIGKHFLSAKKF-NH2) was synthesized as previously described [ ] using the 9-fluorenylmethoxycarbonyl (Fmoc) solid-phase method on Rink amide 4-methyl benzhydrylamine resin (0.55 mmol/g; Novabiochem, Darmstadt, Germany) with a Liberty microwave peptide synthesizer (CEM Co., Matthews, NC, USA).

    Techniques: Adsorption

    Dose-response curve of baltikinin on rat tail arterial smooth muscle preparations after phenylephrine (1 mM) pre-contraction. Each point was plotted as negative tension changes and represents the mean ± SEM ( n = 7). The EC 50 values of baltikinin and BK were 7.16 nM and 1.29 nM, respectively.

    Journal: Toxins

    Article Title: Baltikinin: A New Myotropic Tryptophyllin-3 Peptide Isolated from the Skin Secretion of the Purple-Sided Leaf Frog, Phyllomedusa baltea

    doi: 10.3390/toxins8070213

    Figure Lengend Snippet: Dose-response curve of baltikinin on rat tail arterial smooth muscle preparations after phenylephrine (1 mM) pre-contraction. Each point was plotted as negative tension changes and represents the mean ± SEM ( n = 7). The EC 50 values of baltikinin and BK were 7.16 nM and 1.29 nM, respectively.

    Article Snippet: Peptide Synthesis Baltikinin was synthesized automatically using the solid-phase method (Wang-resin, 0.6 mmol/g, Calbiochem-Novabiochem AG, Läufelfingen) and 9 standard fluorenylmethoxycarbonyl (Fmoc) chemistry (double couplings with 8 equivalent of Fmoc-amino acid derivatives) using a PS3 automated solid phase peptide synthesizer (Protein Technologies, Tucson, AZ, USA).

    Techniques:

    Reversed-phase HPLC chromatogram of skin secretion from the purple-sided leaf frog, Phyllomedusa baltea, with an arrow indicating the elution position/retention time of baltikinin.

    Journal: Toxins

    Article Title: Baltikinin: A New Myotropic Tryptophyllin-3 Peptide Isolated from the Skin Secretion of the Purple-Sided Leaf Frog, Phyllomedusa baltea

    doi: 10.3390/toxins8070213

    Figure Lengend Snippet: Reversed-phase HPLC chromatogram of skin secretion from the purple-sided leaf frog, Phyllomedusa baltea, with an arrow indicating the elution position/retention time of baltikinin.

    Article Snippet: Peptide Synthesis Baltikinin was synthesized automatically using the solid-phase method (Wang-resin, 0.6 mmol/g, Calbiochem-Novabiochem AG, Läufelfingen) and 9 standard fluorenylmethoxycarbonyl (Fmoc) chemistry (double couplings with 8 equivalent of Fmoc-amino acid derivatives) using a PS3 automated solid phase peptide synthesizer (Protein Technologies, Tucson, AZ, USA).

    Techniques: High Performance Liquid Chromatography

    Tandem mass spectrometry (MS/MS) spectrum of the predicted peptide, baltikinin, in the HPLC fraction. Series of b (blue) and y (red) ions of the candidate peptide were observed. The amino acid sequence is shown at the top of the spectrum.

    Journal: Toxins

    Article Title: Baltikinin: A New Myotropic Tryptophyllin-3 Peptide Isolated from the Skin Secretion of the Purple-Sided Leaf Frog, Phyllomedusa baltea

    doi: 10.3390/toxins8070213

    Figure Lengend Snippet: Tandem mass spectrometry (MS/MS) spectrum of the predicted peptide, baltikinin, in the HPLC fraction. Series of b (blue) and y (red) ions of the candidate peptide were observed. The amino acid sequence is shown at the top of the spectrum.

    Article Snippet: Peptide Synthesis Baltikinin was synthesized automatically using the solid-phase method (Wang-resin, 0.6 mmol/g, Calbiochem-Novabiochem AG, Läufelfingen) and 9 standard fluorenylmethoxycarbonyl (Fmoc) chemistry (double couplings with 8 equivalent of Fmoc-amino acid derivatives) using a PS3 automated solid phase peptide synthesizer (Protein Technologies, Tucson, AZ, USA).

    Techniques: Mass Spectrometry, High Performance Liquid Chromatography, Sequencing

    Nucleotide and translated open reading frame amino acid sequence of baltikinin precursor encoding cDNA from the skin secretion of the purple-sided leaf frog, Phyllomedusa baltea . The putative signal peptide sequence is double-underlined, the mature peptide sequence is single-underlined and the stop codon is indicated by an asterisk.

    Journal: Toxins

    Article Title: Baltikinin: A New Myotropic Tryptophyllin-3 Peptide Isolated from the Skin Secretion of the Purple-Sided Leaf Frog, Phyllomedusa baltea

    doi: 10.3390/toxins8070213

    Figure Lengend Snippet: Nucleotide and translated open reading frame amino acid sequence of baltikinin precursor encoding cDNA from the skin secretion of the purple-sided leaf frog, Phyllomedusa baltea . The putative signal peptide sequence is double-underlined, the mature peptide sequence is single-underlined and the stop codon is indicated by an asterisk.

    Article Snippet: Peptide Synthesis Baltikinin was synthesized automatically using the solid-phase method (Wang-resin, 0.6 mmol/g, Calbiochem-Novabiochem AG, Läufelfingen) and 9 standard fluorenylmethoxycarbonyl (Fmoc) chemistry (double couplings with 8 equivalent of Fmoc-amino acid derivatives) using a PS3 automated solid phase peptide synthesizer (Protein Technologies, Tucson, AZ, USA).

    Techniques: Sequencing

    PAGE analysis of reactions 1–3 from Table 1 . The coupling reagents used in lanes 1, 2, and 3 are HBTU, PyBOP, and DMTMM, respectively. As demonstrated by the control lane, starting material (SM) is below the slower-moving peptide-oligonucleotide conjugate (POC).

    Journal: Journal of Nucleic Acids

    Article Title: Coupling Strategies for the Synthesis of Peptide-Oligonucleotide Conjugates for Patterned Synthetic Biomineralization

    doi: 10.4061/2011/926595

    Figure Lengend Snippet: PAGE analysis of reactions 1–3 from Table 1 . The coupling reagents used in lanes 1, 2, and 3 are HBTU, PyBOP, and DMTMM, respectively. As demonstrated by the control lane, starting material (SM) is below the slower-moving peptide-oligonucleotide conjugate (POC).

    Article Snippet: Reaction Solvents in Peptide-Oligonucleotide Synthesis Fragment-coupling reactions using PyBOP ((Benzotriazol-1-yloxy) tripyrrolidinophosphonium hexafluorophosphate; Aldrich) and HBTU were run completely in DMF using DNA immobilized on DEAE Sepharose media (DFF-100, Sigma).

    Techniques: Polyacrylamide Gel Electrophoresis