Cyclizing Disulfide-Rich Peptides Using Sortase A

Akello J Agwa, David J Craik, Christina I Schroeder

Research output: Chapter or section in a book/report/conference proceedingChapter or section

4 Citations (SciVal)


Sortase A (SrtA) is an enzyme obtained from Staphylococcus aureus that catalyzes site-specific transpeptidation of surface proteins to the bacterial cell membrane. SrtA recognizes an LPXTG amino acid motif and cleaves between the Thr and Gly to form a thioester-linked acyl-enzyme intermediate. The intermediate is resolved in the presence of a nucleophilic N-terminal polyglycine resulting in ligation of the acyl donor to the polyglycine acceptor. Here we describe the application of SrtA as a tool for the cyclization of disulfide-rich peptides. Reactions are typically tailored to each disulfide-rich peptide with optimal conditions producing yields of 40-50% cyclized peptide.

Original languageEnglish
Title of host publicationEnzyme-Mediated Ligation Methods
EditorsM Schmidt, T Nuijens
Place of PublicationNew York
Number of pages13
ISBN (Electronic)978-1-4939-9546-2
ISBN (Print)978-1-4939-9545-5
Publication statusPublished - 30 Jun 2019

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029


  • Cyclization
  • Cyclotide
  • Head-to-tail cyclic peptide
  • Kalata B1
  • Macrocycle
  • Peptide ligation
  • Semienzymatic
  • Sortase A

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics


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