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Identification of Highly Reactive Sequences For PLP-Mediated Bioconjugation Using a Combinatorial Peptide Library

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    Identification of Highly Reactive Sequences For PLP-Mediated Bioconjugation Using a Combinatorial Peptide Library
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    • Leah S. Witus
      Leah S. Witus
      Department of Chemistry, University of California, Berkeley, California 94720-1460, United States, Materials Sciences Division, Lawrence Berkeley National Laboratories, Berkeley, California 94720-1460, United States, and QB3/Chemistry Mass Spectrometry Facility, University of California, Berkeley, California 94720-1460, United States
      More by Leah S. Witus
    • Troy Moore
      Troy Moore
      Department of Chemistry, University of California, Berkeley, California 94720-1460, United States, Materials Sciences Division, Lawrence Berkeley National Laboratories, Berkeley, California 94720-1460, United States, and QB3/Chemistry Mass Spectrometry Facility, University of California, Berkeley, California 94720-1460, United States
      More by Troy Moore
    • B W. Thuronyi
      B W. Thuronyi
      Department of Chemistry, University of California, Berkeley, California 94720-1460, United States, Materials Sciences Division, Lawrence Berkeley National Laboratories, Berkeley, California 94720-1460, United States, and QB3/Chemistry Mass Spectrometry Facility, University of California, Berkeley, California 94720-1460, United States
      More by B W. Thuronyi
    • Aaron P. Esser-Kahn
      Aaron P. Esser-Kahn
      Department of Chemistry, University of California, Berkeley, California 94720-1460, United States, Materials Sciences Division, Lawrence Berkeley National Laboratories, Berkeley, California 94720-1460, United States, and QB3/Chemistry Mass Spectrometry Facility, University of California, Berkeley, California 94720-1460, United States
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    • Rebecca A. Scheck
      Rebecca A. Scheck
      Department of Chemistry, University of California, Berkeley, California 94720-1460, United States, Materials Sciences Division, Lawrence Berkeley National Laboratories, Berkeley, California 94720-1460, United States, and QB3/Chemistry Mass Spectrometry Facility, University of California, Berkeley, California 94720-1460, United States
      More by Rebecca A. Scheck
    • Anthony T. Iavarone
      Anthony T. Iavarone
      Department of Chemistry, University of California, Berkeley, California 94720-1460, United States, Materials Sciences Division, Lawrence Berkeley National Laboratories, Berkeley, California 94720-1460, United States, and QB3/Chemistry Mass Spectrometry Facility, University of California, Berkeley, California 94720-1460, United States
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    • Matthew B. Francis*
      Matthew B. Francis
      Department of Chemistry, University of California, Berkeley, California 94720-1460, United States, Materials Sciences Division, Lawrence Berkeley National Laboratories, Berkeley, California 94720-1460, United States, and QB3/Chemistry Mass Spectrometry Facility, University of California, Berkeley, California 94720-1460, United States
      [email protected]
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    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 2010, 132, 47, 16812–16817
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    https://doi.org/10.1021/ja105429n
    Published November 10, 2010
    Copyright © 2010 American Chemical Society
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    Abstract

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    Chemical reactions that facilitate the attachment of synthetic groups to proteins are useful tools for the field of chemical biology and enable the incorporation of proteins into new materials. We have previously reported a pyridoxal 5′-phosphate (PLP)-mediated reaction that site-specifically oxidizes the N-terminal amine of a protein to afford a ketone. This unique functional group can then be used to attach a reagent of choice through oxime formation. Since its initial report, we have found that the N-terminal sequence of the protein can significantly influence the overall success of this strategy. To obtain short sequences that lead to optimal conversion levels, an efficient method for the evaluation of all possible N-terminal amino acid combinations was needed. This was achieved by developing a generalizable combinatorial peptide library screening platform suitable for the identification of sequences that display high levels of reactivity toward a desired bioconjugation reaction. In the context of N-terminal transamination, a highly reactive alanine−lysine motif emerged, which was confirmed to promote the modification of peptide substrates with PLP. This sequence was also tested on two protein substrates, leading to substantial increases in reactivity relative to their wild-type termini. This readily encodable tripeptide thus appears to provide a significant improvement in the reliability with which the PLP-mediated bioconjugation reaction can be used. This study also provides an important first example of how synthetic peptide libraries can accelerate the discovery and optimization of protein bioconjugation strategies.

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    49. Christian B. Rosen, Richard L. Kwant, James I. MacDonald, Meera Rao, Matthew B. Francis. Capture and Recycling of Sortase A through Site‐Specific Labeling with Lithocholic Acid. Angewandte Chemie International Edition 2016, 55 (30) , 8585-8589. https://doi.org/10.1002/anie.201602353
    50. Richard J. Spears, Martin A. Fascione. Site-selective incorporation and ligation of protein aldehydes. Organic & Biomolecular Chemistry 2016, 14 (32) , 7622-7638. https://doi.org/10.1039/C6OB00778C
    51. Wenguo Zhao, Fei Liu, Yue Chen, Jing Bai, Weiping Gao. Synthesis of well-defined protein–polymer conjugates for biomedicine. Polymer 2015, 66 , A1-A10. https://doi.org/10.1016/j.polymer.2015.03.054
    52. James I MacDonald, Henrik K Munch, Troy Moore, Matthew B Francis. One-step site-specific modification of native proteins with 2-pyridinecarboxyaldehydes. Nature Chemical Biology 2015, 11 (5) , 326-331. https://doi.org/10.1038/nchembio.1792
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    54. Richard L. Kwant, Jake Jaffe, Peter J. Palmere, Matthew B. Francis. Controlled levels of protein modification through a chromatography-mediated bioconjugation. Chemical Science 2015, 6 (4) , 2596-2601. https://doi.org/10.1039/C4SC03790A
    55. Oleksandr Koniev, Alain Wagner. Developments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation. Chem. Soc. Rev. 2015, 44 (15) , 5495-5551. https://doi.org/10.1039/C5CS00048C
    56. Joo H Kang, Michael Super, Chong Wing Yung, Ryan M Cooper, Karel Domansky, Amanda R Graveline, Tadanori Mammoto, Julia B Berthet, Heather Tobin, Mark J Cartwright, Alexander L Watters, Martin Rottman, Anna Waterhouse, Akiko Mammoto, Nazita Gamini, Melissa J Rodas, Anxhela Kole, Amanda Jiang, Thomas M Valentin, Alexander Diaz, Kazue Takahashi, Donald E Ingber. An extracorporeal blood-cleansing device for sepsis therapy. Nature Medicine 2014, 20 (10) , 1211-1216. https://doi.org/10.1038/nm.3640
    57. Craig S. McKay, M.G. Finn. Click Chemistry in Complex Mixtures: Bioorthogonal Bioconjugation. Chemistry & Biology 2014, 21 (9) , 1075-1101. https://doi.org/10.1016/j.chembiol.2014.09.002
    58. Christian B Rosen, David Rodriguez-Larrea, Hagan Bayley. Single-molecule site-specific detection of protein phosphorylation with a nanopore. Nature Biotechnology 2014, 32 (2) , 179-181. https://doi.org/10.1038/nbt.2799
    59. Allie C. Obermeyer, John B. Jarman, Chawita Netirojjanakul, Kareem El Muslemany, Matthew B. Francis. Mild Bioconjugation Through the Oxidative Coupling of ortho ‐Aminophenols and Anilines with Ferricyanide. Angewandte Chemie International Edition 2014, 53 (4) , 1057-1061. https://doi.org/10.1002/anie.201307386
    60. Allie C. Obermeyer, John B. Jarman, Chawita Netirojjanakul, Kareem El Muslemany, Matthew B. Francis. Mild Bioconjugation Through the Oxidative Coupling of ortho ‐Aminophenols and Anilines with Ferricyanide. Angewandte Chemie 2014, 126 (4) , 1075-1079. https://doi.org/10.1002/ange.201307386
    61. Rajesh Sunasee, Ravin Narain. Covalent and Noncovalent Bioconjugation Strategies. 2014, 1-75. https://doi.org/10.1002/9781118775882.ch1
    62. Paresh Agarwal, Joep van der Weijden, Ellen M. Sletten, David Rabuka, Carolyn R. Bertozzi. A Pictet-Spengler ligation for protein chemical modification. Proceedings of the National Academy of Sciences 2013, 110 (1) , 46-51. https://doi.org/10.1073/pnas.1213186110
    63. Chawita Netirojjanakul, Leah S. Witus, Christopher R. Behrens, Chih-Hisang Weng, Anthony T. Iavarone, Matthew B. Francis. Synthetically modified Fc domains as building blocks for immunotherapy applications. Chem. Sci. 2013, 4 (1) , 266-272. https://doi.org/10.1039/C2SC21365F
    64. Justin A. Modica, Stratos Skarpathiotis, Milan Mrksich. Modular Assembly of Protein Building Blocks To Create Precisely Defined Megamolecules. ChemBioChem 2012, 13 (16) , 2331-2334. https://doi.org/10.1002/cbic.201200501
    65. Nikolett Mihala, Ferenc Hudecz. Amino acid and peptide bioconjugates. 2012, 1-39. https://doi.org/10.1039/9781849734677-00001
    66. Hui-wang Ai. Biochemical analysis with the expanded genetic lexicon. Analytical and Bioanalytical Chemistry 2012, 403 (8) , 2089-2102. https://doi.org/10.1007/s00216-012-5784-2
    67. Nicholas Stephanopoulos, Matthew B Francis. Choosing an effective protein bioconjugation strategy. Nature Chemical Biology 2011, 7 (12) , 876-884. https://doi.org/10.1038/nchembio.720
    68. Toni L. Lamoureaux, David H. Lee. Chemical activation of MEK1 – a redox trigger for evaluating the effects of phosphorylation. Chemical Communications 2011, 47 (30) , 8623. https://doi.org/10.1039/c1cc11745a
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    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 2010, 132, 47, 16812–16817
    Click to copy citationCitation copied!
    https://doi.org/10.1021/ja105429n
    Published November 10, 2010
    Copyright © 2010 American Chemical Society
    Request reuse permissions

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