Interaction of proteins and peptides with modeled artificial surfaces and cell membranes is a fundamental phenomenon in many practical applications for biomaterials, biosensor, and medicine. It is more biologically important to study the disease-related proteins/peptides (e.g. amyloid peptides associated with neurodegenerative diseases including Alzheimer's and diabetes type II) interacting with different biological or artificial surfaces, which provides general insights into the mechanism of protein (mis)folding, aggregation, and its relation to pathological process. In this talk, we marry computational and experimental approaches to study the peptide adsorption, conformational dynamics, and surface interactions of A� and hIAPP amyloid peptides on different surfaces including graphite, mica, self-assembled monolayers, and lipid bilayer. The surface-induced conformation, orientation, aggregation, and adsorption of amyloid peptides and the peptide-induced surface hydration and/or membrane disruption reveal different peptide adsorption and aggregation scenarios on different surfaces, providing a general insight into the understanding of surface interactions of peptide at interface.

Conformation, orientation, and surface interaction of peptides at interfaces

244th National Meeting (2012)

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