Origin of Proteolytic Stability of Peptide-Brush Polymers as Globular Proteomimetics.

ABSTRACT: Peptide-brush polymers (PBPs), wherein every side-chain of the polymers is peptidic, represent a new class of proteomimetic with unusually high proteolytic resistance while maintaining bioactivity. Here, we sought to determine the origin of this behavior and to assess its generality via a combined theory and experimental approach. A series of PBPs with various polymer backbone structures were prepared and examined for their proteolytic stability and bioactivity. We discovered that an increase in the hydrophobicity of the polymer backbones is predictive of an elevation in proteolytic stability of the side-chain peptides. Computer simulations, together with small-angle X-ray scattering (SAXS) analysis, revealed globular morphologies for these polymers, in which pendant peptides condense arou

SUBMITTER: Sun H 

PROVIDER: S-EPMC8704038 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature