solid-phase peptide synthesis Search Results


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  • 99
    Millipore solid phase synthesis
    Solid Phase Synthesis, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 63 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 63 article reviews
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    solid phase synthesis - by Bioz Stars, 2020-04
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    99
    SPSS Inc solid phase peptide synthesis
    <t>Solid</t> <t>Phase</t> <t>Peptide</t> <t>Synthesis</t> of the linear mutated analogues of MOG 35–55 .
    Solid Phase Peptide Synthesis, supplied by SPSS Inc, used in various techniques. Bioz Stars score: 99/100, based on 2542 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    CS Bio solid phase peptide synthesis
    <t>Solid</t> <t>Phase</t> <t>Peptide</t> <t>Synthesis</t> of the linear mutated analogues of MOG 35–55 .
    Solid Phase Peptide Synthesis, supplied by CS Bio, used in various techniques. Bioz Stars score: 94/100, based on 65 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    GenScript solid phase peptide synthesis
    <t>Solid</t> <t>Phase</t> <t>Peptide</t> <t>Synthesis</t> of the linear mutated analogues of MOG 35–55 .
    Solid Phase Peptide Synthesis, supplied by GenScript, used in various techniques. Bioz Stars score: 91/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    WuXi AppTec solid phase peptide synthesis
    <t>Solid</t> <t>Phase</t> <t>Peptide</t> <t>Synthesis</t> of the linear mutated analogues of MOG 35–55 .
    Solid Phase Peptide Synthesis, supplied by WuXi AppTec, 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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    86
    AnaSpec solid phase synthesis
    <t>Solid</t> <t>Phase</t> <t>Peptide</t> <t>Synthesis</t> of the linear mutated analogues of MOG 35–55 .
    Solid Phase Synthesis, supplied by AnaSpec, used in various techniques. Bioz Stars score: 86/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    New England Peptide solid phase synthesis
    <t>Solid</t> <t>Phase</t> <t>Peptide</t> <t>Synthesis</t> of the linear mutated analogues of MOG 35–55 .
    Solid Phase Synthesis, supplied by New England Peptide, used in various techniques. Bioz Stars score: 94/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Eurofins solid phase peptide synthesis
    <t>Solid</t> <t>Phase</t> <t>Peptide</t> <t>Synthesis</t> of the linear mutated analogues of MOG 35–55 .
    Solid Phase Peptide Synthesis, supplied by Eurofins, used in various techniques. Bioz Stars score: 95/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    AAPPTec solid phase peptide synthesis
    <t>Solid</t> <t>Phase</t> <t>Peptide</t> <t>Synthesis</t> of the linear mutated analogues of MOG 35–55 .
    Solid Phase Peptide Synthesis, supplied by AAPPTec, used in various techniques. Bioz Stars score: 93/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher solid phase peptide synthesis
    <t>Solid</t> <t>Phase</t> <t>Peptide</t> <t>Synthesis</t> of the linear mutated analogues of MOG 35–55 .
    Solid Phase Peptide Synthesis, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 341 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 341 article reviews
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    92
    Iris Biotech solid phase syntheses
    <t>Solid</t> <t>Phase</t> <t>Peptide</t> <t>Synthesis</t> of the linear mutated analogues of MOG 35–55 .
    Solid Phase Syntheses, supplied by Iris Biotech, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    BIOSYNTAN solid phase peptide synthesis
    <t>Solid</t> <t>Phase</t> <t>Peptide</t> <t>Synthesis</t> of the linear mutated analogues of MOG 35–55 .
    Solid Phase Peptide Synthesis, supplied by BIOSYNTAN, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    CEM Corporation solid phase synthesis
    <t>Solid</t> <t>Phase</t> <t>Peptide</t> <t>Synthesis</t> of the linear mutated analogues of MOG 35–55 .
    Solid Phase Synthesis, supplied by CEM Corporation, used in various techniques. Bioz Stars score: 93/100, based on 54 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 54 article reviews
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    87
    Aviva Systems solid phase peptide synthesis
    <t>Solid</t> <t>Phase</t> <t>Peptide</t> <t>Synthesis</t> of the linear mutated analogues of MOG 35–55 .
    Solid Phase Peptide Synthesis, supplied by Aviva Systems, used in various techniques. Bioz Stars score: 87/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    GL Biochem solid phase peptide synthesis
    <t>Solid</t> <t>Phase</t> <t>Peptide</t> <t>Synthesis</t> of the linear mutated analogues of MOG 35–55 .
    Solid Phase Peptide Synthesis, supplied by GL Biochem, used in various techniques. Bioz Stars score: 95/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Fisher Scientific solid phase peptide synthesis
    <t>Solid</t> <t>Phase</t> <t>Peptide</t> <t>Synthesis</t> of the linear mutated analogues of MOG 35–55 .
    Solid Phase Peptide Synthesis, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 91/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    SPSS Inc fmoc solid phase peptide synthesis
    Improved <t>Fmoc</t> <t>SPPS</t> methodology
    Fmoc Solid Phase Peptide Synthesis, supplied by SPSS Inc, used in various techniques. Bioz Stars score: 97/100, based on 343 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    SPSS Inc on resin solid phase peptide synthesis
    Improved <t>Fmoc</t> <t>SPPS</t> methodology
    On Resin Solid Phase Peptide Synthesis, supplied by SPSS Inc, used in various techniques. Bioz Stars score: 93/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    SPSS Inc standard solid phase peptide synthesis
    (Left) Intramolecular CRRL. A <t>peptide</t> (intra-CRRL RGD, ( 6 )) containing the HQAA ( 1 ) and a terminal aminooxy group was synthesized using <t>standard</t> <t>solid</t> <t>phase</t> peptide <t>synthesis.</t> The CRRL strategy was used to generate a cyclic peptide characterized by liquid chromatography and mass spectrometry. (a) Structure of the intra-CRRL RGD ( 6 ) peptide. (b) A mild oxidant Cu 2+ was added in order to oxidize the HQ to BQ followed by rapid intramolecular oxime formation to generate a cyclic peptide ( 7 ). (c) A mild reductant DTT was added to the solution of cyclized RGD peptide ( 7 ) to reduce and therefore cleave the oxime bond to generate the linear peptide ( 8 ). Mass spectrometry characterization of each product in the intramolecular CRRL strategy are shown. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C). (Right) Intermolecular CRRL demonstrating the conjugation of two different peptides. One peptide (inter-CRRL RGD ( 9 )) contains the HQ group, while the other (PREDRVPHSRN) has an oxyamine group. Each are easily synthesized using standard solid phase peptide technology. (a) Inter-CRRL RGD ( 9 ) peptide in PBS before reaction. (b) A mild oxidant Cu 2+ and oxyamine-PREDRVPHSRN were added to the PBS solution of inter-CRRL RGD ( 9 ) peptide to enable rapid intermolecular CRRL conjugation of the two peptides ( 10 ) (PBS, 37.0 °C). (c) The CRRL product peptide ( 10 ) was then selectively cleaved upon treatment of the reductant DTT to yield the linear-RGD peptide ( 11 ). (Bottom) Mass spectrometry characterization of each product in the intermolecular CRRL strategy. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C).
    Standard Solid Phase Peptide Synthesis, supplied by SPSS Inc, used in various techniques. Bioz Stars score: 97/100, based on 136 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    SPSS Inc solid phase peptide synthesis methods
    (Left) Intramolecular CRRL. A <t>peptide</t> (intra-CRRL RGD, ( 6 )) containing the HQAA ( 1 ) and a terminal aminooxy group was synthesized using <t>standard</t> <t>solid</t> <t>phase</t> peptide <t>synthesis.</t> The CRRL strategy was used to generate a cyclic peptide characterized by liquid chromatography and mass spectrometry. (a) Structure of the intra-CRRL RGD ( 6 ) peptide. (b) A mild oxidant Cu 2+ was added in order to oxidize the HQ to BQ followed by rapid intramolecular oxime formation to generate a cyclic peptide ( 7 ). (c) A mild reductant DTT was added to the solution of cyclized RGD peptide ( 7 ) to reduce and therefore cleave the oxime bond to generate the linear peptide ( 8 ). Mass spectrometry characterization of each product in the intramolecular CRRL strategy are shown. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C). (Right) Intermolecular CRRL demonstrating the conjugation of two different peptides. One peptide (inter-CRRL RGD ( 9 )) contains the HQ group, while the other (PREDRVPHSRN) has an oxyamine group. Each are easily synthesized using standard solid phase peptide technology. (a) Inter-CRRL RGD ( 9 ) peptide in PBS before reaction. (b) A mild oxidant Cu 2+ and oxyamine-PREDRVPHSRN were added to the PBS solution of inter-CRRL RGD ( 9 ) peptide to enable rapid intermolecular CRRL conjugation of the two peptides ( 10 ) (PBS, 37.0 °C). (c) The CRRL product peptide ( 10 ) was then selectively cleaved upon treatment of the reductant DTT to yield the linear-RGD peptide ( 11 ). (Bottom) Mass spectrometry characterization of each product in the intermolecular CRRL strategy. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C).
    Solid Phase Peptide Synthesis Methods, supplied by SPSS Inc, used in various techniques. Bioz Stars score: 91/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    SPSS Inc tboc solid phase peptide synthesis
    (Left) Intramolecular CRRL. A <t>peptide</t> (intra-CRRL RGD, ( 6 )) containing the HQAA ( 1 ) and a terminal aminooxy group was synthesized using <t>standard</t> <t>solid</t> <t>phase</t> peptide <t>synthesis.</t> The CRRL strategy was used to generate a cyclic peptide characterized by liquid chromatography and mass spectrometry. (a) Structure of the intra-CRRL RGD ( 6 ) peptide. (b) A mild oxidant Cu 2+ was added in order to oxidize the HQ to BQ followed by rapid intramolecular oxime formation to generate a cyclic peptide ( 7 ). (c) A mild reductant DTT was added to the solution of cyclized RGD peptide ( 7 ) to reduce and therefore cleave the oxime bond to generate the linear peptide ( 8 ). Mass spectrometry characterization of each product in the intramolecular CRRL strategy are shown. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C). (Right) Intermolecular CRRL demonstrating the conjugation of two different peptides. One peptide (inter-CRRL RGD ( 9 )) contains the HQ group, while the other (PREDRVPHSRN) has an oxyamine group. Each are easily synthesized using standard solid phase peptide technology. (a) Inter-CRRL RGD ( 9 ) peptide in PBS before reaction. (b) A mild oxidant Cu 2+ and oxyamine-PREDRVPHSRN were added to the PBS solution of inter-CRRL RGD ( 9 ) peptide to enable rapid intermolecular CRRL conjugation of the two peptides ( 10 ) (PBS, 37.0 °C). (c) The CRRL product peptide ( 10 ) was then selectively cleaved upon treatment of the reductant DTT to yield the linear-RGD peptide ( 11 ). (Bottom) Mass spectrometry characterization of each product in the intermolecular CRRL strategy. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C).
    Tboc Solid Phase Peptide Synthesis, supplied by SPSS Inc, used in various techniques. Bioz Stars score: 85/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 85 stars, based on 6 article reviews
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    96
    SPSS Inc linear solid phase peptide synthesis
    (Left) Intramolecular CRRL. A <t>peptide</t> (intra-CRRL RGD, ( 6 )) containing the HQAA ( 1 ) and a terminal aminooxy group was synthesized using <t>standard</t> <t>solid</t> <t>phase</t> peptide <t>synthesis.</t> The CRRL strategy was used to generate a cyclic peptide characterized by liquid chromatography and mass spectrometry. (a) Structure of the intra-CRRL RGD ( 6 ) peptide. (b) A mild oxidant Cu 2+ was added in order to oxidize the HQ to BQ followed by rapid intramolecular oxime formation to generate a cyclic peptide ( 7 ). (c) A mild reductant DTT was added to the solution of cyclized RGD peptide ( 7 ) to reduce and therefore cleave the oxime bond to generate the linear peptide ( 8 ). Mass spectrometry characterization of each product in the intramolecular CRRL strategy are shown. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C). (Right) Intermolecular CRRL demonstrating the conjugation of two different peptides. One peptide (inter-CRRL RGD ( 9 )) contains the HQ group, while the other (PREDRVPHSRN) has an oxyamine group. Each are easily synthesized using standard solid phase peptide technology. (a) Inter-CRRL RGD ( 9 ) peptide in PBS before reaction. (b) A mild oxidant Cu 2+ and oxyamine-PREDRVPHSRN were added to the PBS solution of inter-CRRL RGD ( 9 ) peptide to enable rapid intermolecular CRRL conjugation of the two peptides ( 10 ) (PBS, 37.0 °C). (c) The CRRL product peptide ( 10 ) was then selectively cleaved upon treatment of the reductant DTT to yield the linear-RGD peptide ( 11 ). (Bottom) Mass spectrometry characterization of each product in the intermolecular CRRL strategy. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C).
    Linear Solid Phase Peptide Synthesis, supplied by SPSS Inc, used in various techniques. Bioz Stars score: 96/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 96 stars, based on 23 article reviews
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    88
    SPSS Inc classical solid phase peptide synthesis
    (Left) Intramolecular CRRL. A <t>peptide</t> (intra-CRRL RGD, ( 6 )) containing the HQAA ( 1 ) and a terminal aminooxy group was synthesized using <t>standard</t> <t>solid</t> <t>phase</t> peptide <t>synthesis.</t> The CRRL strategy was used to generate a cyclic peptide characterized by liquid chromatography and mass spectrometry. (a) Structure of the intra-CRRL RGD ( 6 ) peptide. (b) A mild oxidant Cu 2+ was added in order to oxidize the HQ to BQ followed by rapid intramolecular oxime formation to generate a cyclic peptide ( 7 ). (c) A mild reductant DTT was added to the solution of cyclized RGD peptide ( 7 ) to reduce and therefore cleave the oxime bond to generate the linear peptide ( 8 ). Mass spectrometry characterization of each product in the intramolecular CRRL strategy are shown. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C). (Right) Intermolecular CRRL demonstrating the conjugation of two different peptides. One peptide (inter-CRRL RGD ( 9 )) contains the HQ group, while the other (PREDRVPHSRN) has an oxyamine group. Each are easily synthesized using standard solid phase peptide technology. (a) Inter-CRRL RGD ( 9 ) peptide in PBS before reaction. (b) A mild oxidant Cu 2+ and oxyamine-PREDRVPHSRN were added to the PBS solution of inter-CRRL RGD ( 9 ) peptide to enable rapid intermolecular CRRL conjugation of the two peptides ( 10 ) (PBS, 37.0 °C). (c) The CRRL product peptide ( 10 ) was then selectively cleaved upon treatment of the reductant DTT to yield the linear-RGD peptide ( 11 ). (Bottom) Mass spectrometry characterization of each product in the intermolecular CRRL strategy. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C).
    Classical Solid Phase Peptide Synthesis, supplied by SPSS Inc, used in various techniques. Bioz Stars score: 88/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    SPSS Inc manual solid phase peptide synthesis
    (Left) Intramolecular CRRL. A <t>peptide</t> (intra-CRRL RGD, ( 6 )) containing the HQAA ( 1 ) and a terminal aminooxy group was synthesized using <t>standard</t> <t>solid</t> <t>phase</t> peptide <t>synthesis.</t> The CRRL strategy was used to generate a cyclic peptide characterized by liquid chromatography and mass spectrometry. (a) Structure of the intra-CRRL RGD ( 6 ) peptide. (b) A mild oxidant Cu 2+ was added in order to oxidize the HQ to BQ followed by rapid intramolecular oxime formation to generate a cyclic peptide ( 7 ). (c) A mild reductant DTT was added to the solution of cyclized RGD peptide ( 7 ) to reduce and therefore cleave the oxime bond to generate the linear peptide ( 8 ). Mass spectrometry characterization of each product in the intramolecular CRRL strategy are shown. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C). (Right) Intermolecular CRRL demonstrating the conjugation of two different peptides. One peptide (inter-CRRL RGD ( 9 )) contains the HQ group, while the other (PREDRVPHSRN) has an oxyamine group. Each are easily synthesized using standard solid phase peptide technology. (a) Inter-CRRL RGD ( 9 ) peptide in PBS before reaction. (b) A mild oxidant Cu 2+ and oxyamine-PREDRVPHSRN were added to the PBS solution of inter-CRRL RGD ( 9 ) peptide to enable rapid intermolecular CRRL conjugation of the two peptides ( 10 ) (PBS, 37.0 °C). (c) The CRRL product peptide ( 10 ) was then selectively cleaved upon treatment of the reductant DTT to yield the linear-RGD peptide ( 11 ). (Bottom) Mass spectrometry characterization of each product in the intermolecular CRRL strategy. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C).
    Manual Solid Phase Peptide Synthesis, supplied by SPSS Inc, used in various techniques. Bioz Stars score: 94/100, based on 47 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    SPSS Inc general solid phase peptide synthesis
    (Left) Intramolecular CRRL. A <t>peptide</t> (intra-CRRL RGD, ( 6 )) containing the HQAA ( 1 ) and a terminal aminooxy group was synthesized using <t>standard</t> <t>solid</t> <t>phase</t> peptide <t>synthesis.</t> The CRRL strategy was used to generate a cyclic peptide characterized by liquid chromatography and mass spectrometry. (a) Structure of the intra-CRRL RGD ( 6 ) peptide. (b) A mild oxidant Cu 2+ was added in order to oxidize the HQ to BQ followed by rapid intramolecular oxime formation to generate a cyclic peptide ( 7 ). (c) A mild reductant DTT was added to the solution of cyclized RGD peptide ( 7 ) to reduce and therefore cleave the oxime bond to generate the linear peptide ( 8 ). Mass spectrometry characterization of each product in the intramolecular CRRL strategy are shown. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C). (Right) Intermolecular CRRL demonstrating the conjugation of two different peptides. One peptide (inter-CRRL RGD ( 9 )) contains the HQ group, while the other (PREDRVPHSRN) has an oxyamine group. Each are easily synthesized using standard solid phase peptide technology. (a) Inter-CRRL RGD ( 9 ) peptide in PBS before reaction. (b) A mild oxidant Cu 2+ and oxyamine-PREDRVPHSRN were added to the PBS solution of inter-CRRL RGD ( 9 ) peptide to enable rapid intermolecular CRRL conjugation of the two peptides ( 10 ) (PBS, 37.0 °C). (c) The CRRL product peptide ( 10 ) was then selectively cleaved upon treatment of the reductant DTT to yield the linear-RGD peptide ( 11 ). (Bottom) Mass spectrometry characterization of each product in the intermolecular CRRL strategy. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C).
    General Solid Phase Peptide Synthesis, supplied by SPSS Inc, used in various techniques. Bioz Stars score: 92/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    SPSS Inc automatic solid phase peptide synthesis
    (Left) Intramolecular CRRL. A <t>peptide</t> (intra-CRRL RGD, ( 6 )) containing the HQAA ( 1 ) and a terminal aminooxy group was synthesized using <t>standard</t> <t>solid</t> <t>phase</t> peptide <t>synthesis.</t> The CRRL strategy was used to generate a cyclic peptide characterized by liquid chromatography and mass spectrometry. (a) Structure of the intra-CRRL RGD ( 6 ) peptide. (b) A mild oxidant Cu 2+ was added in order to oxidize the HQ to BQ followed by rapid intramolecular oxime formation to generate a cyclic peptide ( 7 ). (c) A mild reductant DTT was added to the solution of cyclized RGD peptide ( 7 ) to reduce and therefore cleave the oxime bond to generate the linear peptide ( 8 ). Mass spectrometry characterization of each product in the intramolecular CRRL strategy are shown. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C). (Right) Intermolecular CRRL demonstrating the conjugation of two different peptides. One peptide (inter-CRRL RGD ( 9 )) contains the HQ group, while the other (PREDRVPHSRN) has an oxyamine group. Each are easily synthesized using standard solid phase peptide technology. (a) Inter-CRRL RGD ( 9 ) peptide in PBS before reaction. (b) A mild oxidant Cu 2+ and oxyamine-PREDRVPHSRN were added to the PBS solution of inter-CRRL RGD ( 9 ) peptide to enable rapid intermolecular CRRL conjugation of the two peptides ( 10 ) (PBS, 37.0 °C). (c) The CRRL product peptide ( 10 ) was then selectively cleaved upon treatment of the reductant DTT to yield the linear-RGD peptide ( 11 ). (Bottom) Mass spectrometry characterization of each product in the intermolecular CRRL strategy. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C).
    Automatic Solid Phase Peptide Synthesis, supplied by SPSS Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    SPSS Inc combinatorial solid phase peptide synthesis
    (Left) Intramolecular CRRL. A <t>peptide</t> (intra-CRRL RGD, ( 6 )) containing the HQAA ( 1 ) and a terminal aminooxy group was synthesized using <t>standard</t> <t>solid</t> <t>phase</t> peptide <t>synthesis.</t> The CRRL strategy was used to generate a cyclic peptide characterized by liquid chromatography and mass spectrometry. (a) Structure of the intra-CRRL RGD ( 6 ) peptide. (b) A mild oxidant Cu 2+ was added in order to oxidize the HQ to BQ followed by rapid intramolecular oxime formation to generate a cyclic peptide ( 7 ). (c) A mild reductant DTT was added to the solution of cyclized RGD peptide ( 7 ) to reduce and therefore cleave the oxime bond to generate the linear peptide ( 8 ). Mass spectrometry characterization of each product in the intramolecular CRRL strategy are shown. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C). (Right) Intermolecular CRRL demonstrating the conjugation of two different peptides. One peptide (inter-CRRL RGD ( 9 )) contains the HQ group, while the other (PREDRVPHSRN) has an oxyamine group. Each are easily synthesized using standard solid phase peptide technology. (a) Inter-CRRL RGD ( 9 ) peptide in PBS before reaction. (b) A mild oxidant Cu 2+ and oxyamine-PREDRVPHSRN were added to the PBS solution of inter-CRRL RGD ( 9 ) peptide to enable rapid intermolecular CRRL conjugation of the two peptides ( 10 ) (PBS, 37.0 °C). (c) The CRRL product peptide ( 10 ) was then selectively cleaved upon treatment of the reductant DTT to yield the linear-RGD peptide ( 11 ). (Bottom) Mass spectrometry characterization of each product in the intermolecular CRRL strategy. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C).
    Combinatorial Solid Phase Peptide Synthesis, supplied by SPSS Inc, used in various techniques. Bioz Stars score: 86/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    SPSS Inc powerful solid phase peptide synthesis
    (Left) Intramolecular CRRL. A <t>peptide</t> (intra-CRRL RGD, ( 6 )) containing the HQAA ( 1 ) and a terminal aminooxy group was synthesized using <t>standard</t> <t>solid</t> <t>phase</t> peptide <t>synthesis.</t> The CRRL strategy was used to generate a cyclic peptide characterized by liquid chromatography and mass spectrometry. (a) Structure of the intra-CRRL RGD ( 6 ) peptide. (b) A mild oxidant Cu 2+ was added in order to oxidize the HQ to BQ followed by rapid intramolecular oxime formation to generate a cyclic peptide ( 7 ). (c) A mild reductant DTT was added to the solution of cyclized RGD peptide ( 7 ) to reduce and therefore cleave the oxime bond to generate the linear peptide ( 8 ). Mass spectrometry characterization of each product in the intramolecular CRRL strategy are shown. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C). (Right) Intermolecular CRRL demonstrating the conjugation of two different peptides. One peptide (inter-CRRL RGD ( 9 )) contains the HQ group, while the other (PREDRVPHSRN) has an oxyamine group. Each are easily synthesized using standard solid phase peptide technology. (a) Inter-CRRL RGD ( 9 ) peptide in PBS before reaction. (b) A mild oxidant Cu 2+ and oxyamine-PREDRVPHSRN were added to the PBS solution of inter-CRRL RGD ( 9 ) peptide to enable rapid intermolecular CRRL conjugation of the two peptides ( 10 ) (PBS, 37.0 °C). (c) The CRRL product peptide ( 10 ) was then selectively cleaved upon treatment of the reductant DTT to yield the linear-RGD peptide ( 11 ). (Bottom) Mass spectrometry characterization of each product in the intermolecular CRRL strategy. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C).
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    Dalton Pharma standard solid phase peptide synthesis
    (Left) Intramolecular CRRL. A <t>peptide</t> (intra-CRRL RGD, ( 6 )) containing the HQAA ( 1 ) and a terminal aminooxy group was synthesized using <t>standard</t> <t>solid</t> <t>phase</t> peptide <t>synthesis.</t> The CRRL strategy was used to generate a cyclic peptide characterized by liquid chromatography and mass spectrometry. (a) Structure of the intra-CRRL RGD ( 6 ) peptide. (b) A mild oxidant Cu 2+ was added in order to oxidize the HQ to BQ followed by rapid intramolecular oxime formation to generate a cyclic peptide ( 7 ). (c) A mild reductant DTT was added to the solution of cyclized RGD peptide ( 7 ) to reduce and therefore cleave the oxime bond to generate the linear peptide ( 8 ). Mass spectrometry characterization of each product in the intramolecular CRRL strategy are shown. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C). (Right) Intermolecular CRRL demonstrating the conjugation of two different peptides. One peptide (inter-CRRL RGD ( 9 )) contains the HQ group, while the other (PREDRVPHSRN) has an oxyamine group. Each are easily synthesized using standard solid phase peptide technology. (a) Inter-CRRL RGD ( 9 ) peptide in PBS before reaction. (b) A mild oxidant Cu 2+ and oxyamine-PREDRVPHSRN were added to the PBS solution of inter-CRRL RGD ( 9 ) peptide to enable rapid intermolecular CRRL conjugation of the two peptides ( 10 ) (PBS, 37.0 °C). (c) The CRRL product peptide ( 10 ) was then selectively cleaved upon treatment of the reductant DTT to yield the linear-RGD peptide ( 11 ). (Bottom) Mass spectrometry characterization of each product in the intermolecular CRRL strategy. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C).
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    (Left) Intramolecular CRRL. A <t>peptide</t> (intra-CRRL RGD, ( 6 )) containing the HQAA ( 1 ) and a terminal aminooxy group was synthesized using <t>standard</t> <t>solid</t> <t>phase</t> peptide <t>synthesis.</t> The CRRL strategy was used to generate a cyclic peptide characterized by liquid chromatography and mass spectrometry. (a) Structure of the intra-CRRL RGD ( 6 ) peptide. (b) A mild oxidant Cu 2+ was added in order to oxidize the HQ to BQ followed by rapid intramolecular oxime formation to generate a cyclic peptide ( 7 ). (c) A mild reductant DTT was added to the solution of cyclized RGD peptide ( 7 ) to reduce and therefore cleave the oxime bond to generate the linear peptide ( 8 ). Mass spectrometry characterization of each product in the intramolecular CRRL strategy are shown. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C). (Right) Intermolecular CRRL demonstrating the conjugation of two different peptides. One peptide (inter-CRRL RGD ( 9 )) contains the HQ group, while the other (PREDRVPHSRN) has an oxyamine group. Each are easily synthesized using standard solid phase peptide technology. (a) Inter-CRRL RGD ( 9 ) peptide in PBS before reaction. (b) A mild oxidant Cu 2+ and oxyamine-PREDRVPHSRN were added to the PBS solution of inter-CRRL RGD ( 9 ) peptide to enable rapid intermolecular CRRL conjugation of the two peptides ( 10 ) (PBS, 37.0 °C). (c) The CRRL product peptide ( 10 ) was then selectively cleaved upon treatment of the reductant DTT to yield the linear-RGD peptide ( 11 ). (Bottom) Mass spectrometry characterization of each product in the intermolecular CRRL strategy. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C).
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    (Left) Intramolecular CRRL. A <t>peptide</t> (intra-CRRL RGD, ( 6 )) containing the HQAA ( 1 ) and a terminal aminooxy group was synthesized using <t>standard</t> <t>solid</t> <t>phase</t> peptide <t>synthesis.</t> The CRRL strategy was used to generate a cyclic peptide characterized by liquid chromatography and mass spectrometry. (a) Structure of the intra-CRRL RGD ( 6 ) peptide. (b) A mild oxidant Cu 2+ was added in order to oxidize the HQ to BQ followed by rapid intramolecular oxime formation to generate a cyclic peptide ( 7 ). (c) A mild reductant DTT was added to the solution of cyclized RGD peptide ( 7 ) to reduce and therefore cleave the oxime bond to generate the linear peptide ( 8 ). Mass spectrometry characterization of each product in the intramolecular CRRL strategy are shown. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C). (Right) Intermolecular CRRL demonstrating the conjugation of two different peptides. One peptide (inter-CRRL RGD ( 9 )) contains the HQ group, while the other (PREDRVPHSRN) has an oxyamine group. Each are easily synthesized using standard solid phase peptide technology. (a) Inter-CRRL RGD ( 9 ) peptide in PBS before reaction. (b) A mild oxidant Cu 2+ and oxyamine-PREDRVPHSRN were added to the PBS solution of inter-CRRL RGD ( 9 ) peptide to enable rapid intermolecular CRRL conjugation of the two peptides ( 10 ) (PBS, 37.0 °C). (c) The CRRL product peptide ( 10 ) was then selectively cleaved upon treatment of the reductant DTT to yield the linear-RGD peptide ( 11 ). (Bottom) Mass spectrometry characterization of each product in the intermolecular CRRL strategy. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C).
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    Image Search Results


    Solid Phase Peptide Synthesis of the linear mutated analogues of MOG 35–55 .

    Journal: Molecules

    Article Title: Rational Design and Synthesis of Altered Peptide Ligands based on Human Myelin Oligodendrocyte Glycoprotein 35–55 Epitope: Inhibition of Chronic Experimental Autoimmune Encephalomyelitis in Mice

    doi: 10.3390/molecules191117968

    Figure Lengend Snippet: Solid Phase Peptide Synthesis of the linear mutated analogues of MOG 35–55 .

    Article Snippet: Conventional Solid Phase Peptide Synthesis (SPPS) of Linear Peptides The synthesis of [Ala41 ]MOG35–55 , [Ala41,46 ]MOG35–55 and [TyrOMe40 ]MOG35–55 was performed on CLTR-Cl resin (3 g).

    Techniques:

    Chemical synthesis of polyUbs. Previous method: Regular SPPS for isoUb‐mediated native chemical ligation. This work: HESPPS for isoUb‐mediated native chemical ligation. HESPPS: high‐efficiency solid‐phase peptide synthesis; Ub: ubiquitin.

    Journal: Advanced Science

    Article Title: A Highly Efficient Synthesis of Polyubiquitin Chains

    doi: 10.1002/advs.201800234

    Figure Lengend Snippet: Chemical synthesis of polyUbs. Previous method: Regular SPPS for isoUb‐mediated native chemical ligation. This work: HESPPS for isoUb‐mediated native chemical ligation. HESPPS: high‐efficiency solid‐phase peptide synthesis; Ub: ubiquitin.

    Article Snippet: Aided by unconventional resin and pseudoproline, they successfully obtained isopeptide‐linked 76‐mer isoUb using regular solid‐phase peptide synthesis (SPPS) techniques.

    Techniques: Ligation

    Site-specific incorporation of thioamides using solid phase peptide synthesis (SPPS). (A) Thioacylbenzotriazole monomers can be synthesized in three steps from Fmoc-protected amino acids using Lawesson’s Reagent or P 4 S 10 to thionate. (B) The thioacylbenzotriazoles can be used to introduce the thioamide during SPPS with minor modifications of standard coupling, deprotection, and cleavage protocols.

    Journal: ACS chemical biology

    Article Title: Thioamides: Biosynthesis of Natural Compounds and Chemical Applications

    doi: 10.1021/acschembio.8b01022

    Figure Lengend Snippet: Site-specific incorporation of thioamides using solid phase peptide synthesis (SPPS). (A) Thioacylbenzotriazole monomers can be synthesized in three steps from Fmoc-protected amino acids using Lawesson’s Reagent or P 4 S 10 to thionate. (B) The thioacylbenzotriazoles can be used to introduce the thioamide during SPPS with minor modifications of standard coupling, deprotection, and cleavage protocols.

    Article Snippet: While the aforementioned benzotriazole synthesis can be used for Boc- or Fmoc- based precursors, thioamides are incompatible with the harsh HF cleavage used in Boc-based solid phase peptide synthesis (SPPS).

    Techniques: Synthesized, Introduce

    Synthesis of the TuAcK-containing compound 1 . Reagents: (i) Fmoc-based SPPS; (ii) 85% (v/v) TFA in DCM; (iii) Thiophosgene (CSCl 2 ), Et 3 N; (iv) 7 N NH 3 in MeOH.

    Journal: Bioorganic & medicinal chemistry letters

    Article Title: A mechanism-based potent sirtuin inhibitor containing Nε-thiocarbamoyl-lysine (TuAcK)

    doi: 10.1016/j.bmcl.2011.06.069

    Figure Lengend Snippet: Synthesis of the TuAcK-containing compound 1 . Reagents: (i) Fmoc-based SPPS; (ii) 85% (v/v) TFA in DCM; (iii) Thiophosgene (CSCl 2 ), Et 3 N; (iv) 7 N NH 3 in MeOH.

    Article Snippet: Synthesis of compound 1 ( ). (a) The solid phase synthesis part of the synthesis of this compound was performed with the Fmoc chemistry-based solid phase peptide synthesis (SPPS) at a 0.05 mmol scale on a PS3 peptide synthesizer (Protein Technologies Inc., Tucson, AZ, USA) from Rink Amide AM resin.

    Techniques:

    Improved Fmoc SPPS methodology

    Journal: Journal of Chemical Biology

    Article Title: Synthesis of biologically important neutral amylo-β peptide by using improved Fmoc solid-phase peptide synthetic strategy

    doi: 10.1007/s12154-015-0128-2

    Figure Lengend Snippet: Improved Fmoc SPPS methodology

    Article Snippet: The most essential biologically active neutral amylo-β peptide (KVKRIILARS) was successfully synthesized, and some synthetic modification was performed using the Fmoc solid-phase peptide synthesis (SPPS) method for purity and yield improvement.

    Techniques:

    Preparation of novel histone H3 peptide-based LSD1 inactivators 2a – c with γ-turn inducers by Fmoc-based SPPS (Boc-Ala-OH was used as the N -terminal amino acid). Reagents and conditions: ( a ) MsCl, Et 3 N in THF; ( b ) PCPA, Et 3 N in H 2 O:CH 3 CN solution; ( c ) TFA, thioanisole, H 2 O; and ( d ) preparative HPLC. Peptide chains shown in italics are protected.

    Journal: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry

    Article Title: Design, Synthesis, and In Vitro Evaluation of Novel Histone H3 Peptide-Based LSD1 Inactivators Incorporating α,α-Disubstituted Amino Acids with γ-Turn-Inducing Structures

    doi: 10.3390/molecules23051099

    Figure Lengend Snippet: Preparation of novel histone H3 peptide-based LSD1 inactivators 2a – c with γ-turn inducers by Fmoc-based SPPS (Boc-Ala-OH was used as the N -terminal amino acid). Reagents and conditions: ( a ) MsCl, Et 3 N in THF; ( b ) PCPA, Et 3 N in H 2 O:CH 3 CN solution; ( c ) TFA, thioanisole, H 2 O; and ( d ) preparative HPLC. Peptide chains shown in italics are protected.

    Article Snippet: Peptides 2 were synthesized by Fmoc-based solid-phase peptide synthesis (SPPS) according to modified previous procedures for histone H3-based peptides [ , , ].

    Techniques: High Performance Liquid Chromatography

    Iterative Fmoc-SPPS of Key Intermediate 6

    Journal: Organic letters

    Article Title: Solid-Phase Synthesis of Lysobactin (Katanosin B): Insights into Structure and Function

    doi: 10.1021/ol300926d

    Figure Lengend Snippet: Iterative Fmoc-SPPS of Key Intermediate 6

    Article Snippet: The natural product was synthesized via a linear approach using mostly Fmoc-strategy solid phase peptide synthesis (SPPS) with a single purification.

    Techniques:

    (Left) Intramolecular CRRL. A peptide (intra-CRRL RGD, ( 6 )) containing the HQAA ( 1 ) and a terminal aminooxy group was synthesized using standard solid phase peptide synthesis. The CRRL strategy was used to generate a cyclic peptide characterized by liquid chromatography and mass spectrometry. (a) Structure of the intra-CRRL RGD ( 6 ) peptide. (b) A mild oxidant Cu 2+ was added in order to oxidize the HQ to BQ followed by rapid intramolecular oxime formation to generate a cyclic peptide ( 7 ). (c) A mild reductant DTT was added to the solution of cyclized RGD peptide ( 7 ) to reduce and therefore cleave the oxime bond to generate the linear peptide ( 8 ). Mass spectrometry characterization of each product in the intramolecular CRRL strategy are shown. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C). (Right) Intermolecular CRRL demonstrating the conjugation of two different peptides. One peptide (inter-CRRL RGD ( 9 )) contains the HQ group, while the other (PREDRVPHSRN) has an oxyamine group. Each are easily synthesized using standard solid phase peptide technology. (a) Inter-CRRL RGD ( 9 ) peptide in PBS before reaction. (b) A mild oxidant Cu 2+ and oxyamine-PREDRVPHSRN were added to the PBS solution of inter-CRRL RGD ( 9 ) peptide to enable rapid intermolecular CRRL conjugation of the two peptides ( 10 ) (PBS, 37.0 °C). (c) The CRRL product peptide ( 10 ) was then selectively cleaved upon treatment of the reductant DTT to yield the linear-RGD peptide ( 11 ). (Bottom) Mass spectrometry characterization of each product in the intermolecular CRRL strategy. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C).

    Journal: Bioconjugate Chemistry

    Article Title: General Chemoselective and Redox-Responsive Ligation and Release Strategy

    doi: 10.1021/bc400565y

    Figure Lengend Snippet: (Left) Intramolecular CRRL. A peptide (intra-CRRL RGD, ( 6 )) containing the HQAA ( 1 ) and a terminal aminooxy group was synthesized using standard solid phase peptide synthesis. The CRRL strategy was used to generate a cyclic peptide characterized by liquid chromatography and mass spectrometry. (a) Structure of the intra-CRRL RGD ( 6 ) peptide. (b) A mild oxidant Cu 2+ was added in order to oxidize the HQ to BQ followed by rapid intramolecular oxime formation to generate a cyclic peptide ( 7 ). (c) A mild reductant DTT was added to the solution of cyclized RGD peptide ( 7 ) to reduce and therefore cleave the oxime bond to generate the linear peptide ( 8 ). Mass spectrometry characterization of each product in the intramolecular CRRL strategy are shown. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C). (Right) Intermolecular CRRL demonstrating the conjugation of two different peptides. One peptide (inter-CRRL RGD ( 9 )) contains the HQ group, while the other (PREDRVPHSRN) has an oxyamine group. Each are easily synthesized using standard solid phase peptide technology. (a) Inter-CRRL RGD ( 9 ) peptide in PBS before reaction. (b) A mild oxidant Cu 2+ and oxyamine-PREDRVPHSRN were added to the PBS solution of inter-CRRL RGD ( 9 ) peptide to enable rapid intermolecular CRRL conjugation of the two peptides ( 10 ) (PBS, 37.0 °C). (c) The CRRL product peptide ( 10 ) was then selectively cleaved upon treatment of the reductant DTT to yield the linear-RGD peptide ( 11 ). (Bottom) Mass spectrometry characterization of each product in the intermolecular CRRL strategy. All of the reactions were performed at physiological conditions (PBS, pH 7.4, 37.0 °C).

    Article Snippet: To conjugate a range of biomolecules using the CRRL strategy, we used standard solid phase peptide synthesis (SPPS) to generate dynamic peptides containing the hydroquinone group at various locations (Figure ).

    Techniques: Synthesized, Liquid Chromatography, Mass Spectrometry, Conjugation Assay

    (a) Synthesis of a protected hydroquinone tethered Fmoc amino acid (HQAA; 1 ) for use in solid phase peptide synthesis to generate peptides containing the hydroquinone group for site-specific CRRL chemistry. (b) Scheme showing how HQAA ( 1 ) can be added to any site within a peptide by applying standard solid phase peptide synthesis technology. This strategy allows for the CRRL method to be incorporated into a variety of biomolecules.

    Journal: Bioconjugate Chemistry

    Article Title: General Chemoselective and Redox-Responsive Ligation and Release Strategy

    doi: 10.1021/bc400565y

    Figure Lengend Snippet: (a) Synthesis of a protected hydroquinone tethered Fmoc amino acid (HQAA; 1 ) for use in solid phase peptide synthesis to generate peptides containing the hydroquinone group for site-specific CRRL chemistry. (b) Scheme showing how HQAA ( 1 ) can be added to any site within a peptide by applying standard solid phase peptide synthesis technology. This strategy allows for the CRRL method to be incorporated into a variety of biomolecules.

    Article Snippet: To conjugate a range of biomolecules using the CRRL strategy, we used standard solid phase peptide synthesis (SPPS) to generate dynamic peptides containing the hydroquinone group at various locations (Figure ).

    Techniques: