Intrinsic Defect Formation in Peptide Self-Assembly

TL;DR

This paper investigates the formation mechanisms of intrinsic defects in peptide self-assembled nanostructures using Monte Carlo simulations, revealing that symmetry breaking during morphological transformation causes defects without affecting chirality.

Contribution

It provides the first systematic analysis of intrinsic defect formation in peptide self-assembly, linking microscopic mismatch to defect emergence.

Findings

Symmetry breaking at layer ends causes defects.

Defect formation is due to mismatch in layer stacking.

Chirality remains unaffected by defects.

Abstract

In contrast to extensively studied defects in traditional materials, we report here for the first time a systematic investigation of the formation mechanism of intrinsic defects in self-assembled peptide nanostructures. The Monte Carlo simulations with our simplified dynamic hierarchical model revealed that the symmetry breaking of layer bending mode at the two ends during morphological transformation is responsible for intrinsic defect formation, whose microscopic origin is the mismatch between layer stacking along the side-chain direction and layer growth along the hydrogen bond direction. Moreover, defect formation does not affect the chirality of the self-assembled structure, which is determined by the initial steps of the peptide self-assembly process.