Unraveling the Atomistic Mechanism of Electrostatic Lateral Association of Peptide β-Sheet Structures and Its Role in Nanofiber Growth and Hydrogelation.

ABSTRACT: Guiding molecular assembly of peptides into rationally engineered nanostructures remains a major hurdle against the development of functional peptide-based nanomaterials. Various non-covalent interactions come into play to drive the formation and stabilization of these assemblies, of which electrostatic interactions are key. Here, the atomistic mechanisms by which electrostatic interactions contribute toward controlling self-assembly and lateral association of ultrashort β-sheet forming peptides are deciphered. Our results show that this is governed by charge distribution and ionic complementarity, both affecting the interaction patterns between charged residues: terminal, core, and/or terminal-to-core attraction/repulsion. Controlling electrostatic interactions enabled fine-tuning nanofib

SUBMITTER: Soliman MAN 

PROVIDER: S-EPMC11817957 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature