@inbook{5cddaec3cb4e4cebb2634cda4d707673,
title = "Cyclizing Disulfide-Rich Peptides Using Sortase A",
abstract = "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.",
keywords = "Cyclization, Cyclotide, Head-to-tail cyclic peptide, Kalata B1, Macrocycle, Peptide ligation, Semienzymatic, Sortase A",
author = "Agwa, {Akello J} and Craik, {David J} and Schroeder, {Christina I}",
year = "2019",
month = jun,
day = "30",
doi = "10.1007/978-1-4939-9546-2_3",
language = "English",
isbn = "978-1-4939-9545-5",
volume = "2012",
series = "Methods in Molecular Biology",
publisher = "Humana Press",
pages = "29--41",
editor = "M Schmidt and T Nuijens",
booktitle = "Enzyme-Mediated Ligation Methods",
address = "USA United States",
}