Sortase A-mediated cyclization of novel polycyclic RGD peptides for ανβ3 integrin targeting

Yajun Chen; Lixuan Jia; Guilan Zhu; Wei Wang; Ming Geng; Hongxia Lu; Yan Zhang; Minghui Zhou; Fangyan Zhang; Xiaozhong Cheng

doi:10.1016/j.bmcl.2022.128888

Sortase A-mediated cyclization of novel polycyclic RGD peptides for α_νβ₃ integrin targeting

Bioorg Med Chem Lett. 2022 Oct 1:73:128888. doi: 10.1016/j.bmcl.2022.128888. Epub 2022 Jul 15.

Authors

Affiliations

¹ Anhui Engineering Laboratory for Medicinal and Food Homologous Natural Resources Exploration, Hefei Normal University, Hefei 230601, China.
² Anhui Engineering Laboratory for Medicinal and Food Homologous Natural Resources Exploration, Hefei Normal University, Hefei 230601, China. Electronic address: chengxiaozhong@hfnu.edu.cn.

PMID: 35839966
DOI: 10.1016/j.bmcl.2022.128888

Abstract

Cyclic arginine-glycine-aspartic (RGD) peptides that specifically bind to integrin α_νβ₃ have been developed for drug delivery, tracers, and imaging for tumor diagnosis and treatment. Herein, a series of polycyclic RGD peptides containing dual, tri, and tetra rings were designed and synthesized through sortase A-mediated ligation. An in vitro test on cell adhesion inhibition indicated that the RGD peptide containing tricylic structure exhibited outstanding potency and selectivity for α_νβ₃ integrin.

Keywords: Adhesion inhibition; Polycyclic RGD peptides; α(ν)β(3) integrin.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Aminoacyltransferases
Bacterial Proteins
Cyclization
Cysteine Endopeptidases
Integrin alphaVbeta3* / metabolism
Integrin beta3* / metabolism
Oligopeptides / chemistry

Substances

Bacterial Proteins
Integrin alphaVbeta3
Integrin beta3
Oligopeptides
arginyl-glycyl-aspartic acid
Aminoacyltransferases
sortase A
Cysteine Endopeptidases