Expressed Protein Selenoester Ligation

Sameer S. Kulkarni, Emma E. Watson, Joshua W.C. Maxwell, Gerhard Niederacher, Jason Johansen-Leete, Susanne Huhmann, Somnath Mukherjee, Alexander R. Norman, Julia Kriegesmann, Christian F.W. Becker, Richard J. Payne

Research output: Contribution to journalArticleResearchpeer-review

24 Citations (Scopus)

Abstract

Herein, we describe the development and application of a novel expressed protein selenoester ligation (EPSL) methodology for the one-pot semi-synthesis of modified proteins. EPSL harnesses the rapid kinetics of ligation reactions between modified synthetic selenopeptides and protein aryl selenoesters (generated from expressed intein fusion precursors) followed by in situ chemoselective deselenization to afford target proteins at concentrations that preclude the use of traditional ligation methods. The utility of the EPSL technology is showcased through the efficient semi-synthesis of ubiquitinated polypeptides, lipidated analogues of the membrane-associated GTPase YPT6, and site-specifically phosphorylated variants of the oligomeric chaperone protein Hsp27 at high dilution.

Original languageEnglish
Article numbere202200163
Number of pages6
JournalAngewandte Chemie - International Edition
Volume61
Issue number20
DOIs
Publication statusPublished - 9 May 2022
Externally publishedYes

Keywords

  • Expressed Protein Selenoesters
  • Peptides
  • Protein Modifications
  • Protein Semi-Synthesis
  • Proteins

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