Interfacial Interactions within Amyloid Protein Corona Based on 2D MoS₂ Nanosheets

Area of Science:

• Nanomaterial-biology interfaces
• Amyloid protein aggregation
• Biophysical chemistry

Background:

• The amyloid protein corona influences nanomaterial biological effects and amyloid disease progression.
• Understanding the interaction between amyloid peptides and nanomaterials is critical.

Purpose of the Study:

• To investigate the nano-bio interface phenomenon between human islet amyloid peptide (hIAPP) and MoS2 nanosheets.
• To elucidate the molecular mechanisms underlying hIAPP interaction and fibrillation on MoS2 surfaces.

Main Methods:

• Utilized theoretical and experimental approaches to study hIAPP-MoS2 interactions.
• Analyzed binding modes, including monomer, dimer, and oligomer interactions.
• Investigated the effect of MoS2 on hIAPP fibrillation kinetics.

Main Results:

• MoS2 nanosheets attract hIAPP via van der Waals forces, altering peptide interactions.
• hIAPP oligomers exhibit a unique "standing" binding mode on MoS2, exposing β-sheet surfaces.
• MoS2 nanosheets accelerate hIAPP fibrillation at specific concentrations, driven by the nano-bio interface.

Conclusions:

• The study provides molecular insights into the nano-bio interface within the amyloid protein corona.
• MoS2-induced hIAPP fibrillation highlights a potential pathway in amyloid disease evolution.
• Findings contribute to understanding nanomaterial interactions with amyloidogenic peptides.