Peptides derived from cadherin juxtamembrane region inhibit platelet function.

ABSTRACT: The juxtamembrane domains (JMD) of transmembrane proteins are rich in critical peptide sequences that participate in dynamic cell signalling events. Synthetic JMD peptides derived from cadherin cell adhesion proteins have previously been shown to modulate platelet function. In this study, we aimed to develop functional bioactive agents from bioinformatically identified critical peptide sequences. We synthesized overlapping 12-15 amino acid peptides from E- and N-cadherin JMD and assessed their effect on platelet aggregation and platelet ATP secretion. Peptides derived from close to the membrane proximal region inhibit platelet function. Sequential deletion of amino acids from the N- and C-termini of the inhibitory E-cadherin peptides identified the short K⁷⁵⁶EPLLP⁷⁶³

SUBMITTER: Golla K 

PROVIDER: S-EPMC6227957 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature