Sortase A-mediated cyclization of novel polycyclic RGD peptides for ???3 integrin targeting

Cyclic arginine-glycine-aspartic (RGD) peptides that specifically bind to integrin alpha nu beta 3 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 alpha nu beta 3 integrin.

Automated summary

Cyclic arginine-glycine-aspartic (RGD) peptides with specific binding ability to integrin alpha nu beta 3 have been developed for drug delivery, tracing, and imaging in tumor diagnosis and treatment. In this study, a series of polycyclic RGD peptides with dual, tri, and tetra rings were designed and synthesized using sortase A-mediated ligation. In vitro cell adhesion inhibition tests revealed that the tricyclic RGD peptide exhibited outstanding potency and selectivity for alpha nu beta 3 integrin.