Enzymatic “Click” Ligation: Selective Cysteine Modification in Polypeptides Enabled by Promiscuous Glutathione S-Transferase

Authors


  • 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.

Abstract

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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.

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