We study how biological and synthetic interfaces, including nanoparticles, surfaces, and soft matter, direct and modulate peptide self-assembly pathways, with a focus on amyloid fibril formation, corona effects, and interface-driven aggregation relevant to neurodegenerative diseases.

We decode how peptide sequence encodes fibril structure, polymorphism, and function. Using molecular simulations and biophysical experiments, we establish sequence–structure–function relationships that guide the rational design of peptide fibrils and hybrid biomaterials for applications in catalysis, regenerative medicine, and biosensing.

We investigate how self-assembling and antimicrobial peptides interact with lipid membranes, exploring how membrane composition, oxidation state, and peptide aggregation govern membrane activity, selectivity, and biological function.