Synergistic anion-π interactions in peptidomimetic polyethers.

ABSTRACT: Anion-π interactions are crucial in various biological processes, such as enzyme catalysis and ion transport. Despite their significance, the exploitation of anion-π interactions in synthetic polymer systems remains underexplored. This study investigates anion-π interactions using chemically well-defined peptidomimetics guided by the composition of mussel foot proteins. Specifically, polyether-based polymers were designed utilizing two functional epoxide monomers-catechol acetonide glycidyl ether and 4,4-dimethyl-2-oxazoline glycidyl ether-to mimic the key amino acids 3,4-dihydroxyphenylalanine and aspartic acid, respectively. A surface forces apparatus was employed to study the anion-π interaction between the polymers, considering the effects of relative monomer composition and pH conditi

SUBMITTER: Lee S 

PROVIDER: S-EPMC11831155 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature