Polyphenol-Mediated Peptide Assembly Modulates Melittin Toxicity: A Structure-Activity Strategy for Neutralizing the Interface Affinity of Pore-Forming Toxins to Cell Membranes.

ABSTRACT: Pore-forming agents can bind at the interface of and permeabilize cell membranes. Understanding and mitigating this mechanism is pragmatic for developing bionanomaterials and strategies against biologically active species that target the cell membrane. Herein, we explore the molecular interactions between melittin, a membrane-active pore-forming peptide from honeybee venom, and a series of structurally similar polyphenols. We sought to better understand the biophysical bases by which pore-forming toxins interact with cell membranes and to establish a materials-based strategy using small molecules to control peptide assembly and biotoxin activity at the membrane interface. Building on our previous discovery that epigallocatechin gallate reduces the membrane affinity of melittin by decreasin

SUBMITTER: Han H 

PROVIDER: S-EPMC12442020 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature