Revisiting ligation at selenomethionine: Insights into native chemical ligation at selenocysteine and homoselenocysteine

Rebecca Notis Dardashti, Norman Metanis*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

Selenomethionine (Sem) has been incorporated recombinantly into proteins many times to elucidate their structure and function. In this paper, we revisit incorporation via chemical protein synthesis to shed light on the mechanism of native chemical ligation. The effect of chalcogen position on ligation is investigated, and selenium-containing peptide ligation is optimized. Additionally, selective methylation is performed on selenolates in a peptide in the presence of unprotected thiols.

Original languageAmerican English
Pages (from-to)4983-4989
Number of pages7
JournalBioorganic and Medicinal Chemistry
Volume25
Issue number18
DOIs
StatePublished - 2017

Bibliographical note

Publisher Copyright:
© 2017 Elsevier Ltd

Keywords

  • Chemical protein synthesis
  • Native chemical ligation
  • Peptide methylation
  • Selenocysteine
  • Selenomethionine

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