Enzymatic “Click” Ligation: Selective Cysteine Modification in Polypeptides Enabled by Promiscuous Glutathione S‐Transferase
2013; Wiley; Volume: 125; Issue: 52 Linguagem: Inglês
10.1002/ange.201306430
ISSN1521-3757
AutoresChi Zhang, Alexander M. Spokoyny, Yekui Zou, Mark D. Simon, Bradley L. Pentelute,
Tópico(s)Monoclonal and Polyclonal Antibodies Research
ResumoAngewandte ChemieVolume 125, Issue 52 p. 14251-14255 Zuschrift Enzymatic "Click" Ligation: Selective Cysteine Modification in Polypeptides Enabled by Promiscuous Glutathione S-Transferase† Chi Zhang, Chi Zhang Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, MA 02139 (USA)Search for more papers by this authorDr. Alexander M. Spokoyny, Dr. Alexander M. Spokoyny Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, MA 02139 (USA)Search for more papers by this authorDr. Yekui Zou, Dr. Yekui Zou Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, MA 02139 (USA)Search for more papers by this authorMark D. Simon, Mark D. Simon Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, MA 02139 (USA)Search for more papers by this authorProf. Dr. Bradley L. Pentelute, Corresponding Author Prof. Dr. Bradley L. Pentelute [email protected] Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, MA 02139 (USA)Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, MA 02139 (USA)Search for more papers by this author Chi Zhang, Chi Zhang Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, MA 02139 (USA)Search for more papers by this authorDr. Alexander M. Spokoyny, Dr. Alexander M. Spokoyny Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, MA 02139 (USA)Search for more papers by this authorDr. Yekui Zou, Dr. Yekui Zou Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, MA 02139 (USA)Search for more papers by this authorMark D. Simon, Mark D. Simon Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, MA 02139 (USA)Search for more papers by this authorProf. Dr. Bradley L. Pentelute, Corresponding Author Prof. Dr. Bradley L. Pentelute [email protected] Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, MA 02139 (USA)Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, MA 02139 (USA)Search for more papers by this author First published: 12 November 2013 https://doi.org/10.1002/ange.201306430Citations: 10 † We thank Prof. Stephen L. Buchwald (S.L.B.) for encouragement and support. This research was generously sponsored by the National Institutes of Health (GM101762 for A.M.S. and GM046059 for S.L.B.) and also supported by MIT start-up funds and a Damon Runyon Cancer Research Foundation award for B.L.P. C.Z. is a recipient of a Amgen Summer Graduate Research Fellowship. The content is solely the responsibility of the authors and does not necessarily represent the official views of the NIH. We are indebted to Rocco Policarpo, Jingjing J. Ling, Dr. Xiaoli Liao, and Amy Rabideau for technical assistance and helpful discussions, and to Prof. R. John Collier (Harvard) for commenting on the manuscript and contributing some of the laboratory equipment used in these studies. We also thank Prof. Stephen B. H. Kent (U. Chicago) for commenting on this manuscript. Read the full textAboutPDF ToolsRequest permissionAdd to favorites ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat Graphical Abstract Sonderbehandlung: Natürliche Glutathion-S-transferase (GST) katalysiert die effiziente "Klick"-Ligation von Polypeptiden mit einer N-terminalen Glutathionsequenz und Biomolekülen oder chemischen Sonden, die perfluorierte aromatische Gruppen tragen (siehe Schema). Die ortsspezifische Modifikation eines Cysteinrests gelingt in Gegenwart anderer nichtgeschützter Cysteinreste und reaktiver funktioneller Gruppen. Supporting Information As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. 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