Development of truncated elastin-like peptide analogues with improved temperature-response and self-assembling properties.

ABSTRACT: Functional peptides, which are composed of proteinogenic natural amino acids, are expected to be used as biomaterials with minimal environmental impact. Synthesizing a functional peptide with a shorter amino acid sequence while retaining its function is a easy and economical strategy. Furthermore, shortening functional peptides helps to elucidate the mechanism of their functional core region. Truncated elastin-like peptides (ELPs) are peptides consisting of repetitive sequences, derived from the elastic protein tropoelastin, that show the thermosensitive formation of coacervates. In this study, to obtain shortened ELP analogues, we synthesized several (Phe-Pro-Gly-Val-Gly)_n (FPGVG)_n analogues with one or two amino acid residues deleted from each repeat sequence, such

SUBMITTER: Sumiyoshi S 

PROVIDER: S-EPMC9653453 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature