Effects of surface interactions on peptide aggregate morphology.

Area of Science:

• Biophysics
• Computational Chemistry
• Materials Science

Background:

• Peptide aggregation is crucial in biological systems and materials science.
• Understanding how surfaces influence peptide assembly is key to controlling aggregate structure.

Purpose of the Study:

• To investigate the role of attractive surfaces in peptide aggregate formation.
• To determine how surface attraction and peptide chain stiffness affect aggregate morphology and stability.

Main Methods:

• Replica exchange molecular dynamics simulations were employed.
• A coarse-grained peptide model was utilized to study aggregation.
• The influence of varying surface attraction and peptide chain stiffness was examined.

Main Results:

• In the absence of a surface, peptide aggregate morphology (amorphous, β-barrels, fibrils) depends on chain stiffness.
• Attractive surfaces favor fibrillar structures, with morphology primarily dictated by surface attraction.
• Both peptide-peptide and peptide-surface interactions cooperatively influence assembly, affecting morphology and transition properties.

Conclusions:

• Attractive surfaces significantly alter peptide aggregation pathways, promoting fibrillar structures.
• Surface attraction and chain stiffness synergistically enhance the frequency and stability of ordered fibrillar aggregates.
• The findings provide insights into surface-mediated self-assembly for potential applications in biomaterials and nanotechnology.