ABSTRACT
Design of bioinspired fibrous materials has many applications both in the development of fundamental science, such as understanding protein folding, protein sequence to structure relationships. This chapter presents a generic, minimalistic water-explicit polarizable protein model (WEPPROM) that can be used to characterize the driving forces behind protein folding and aggregation without the addition of biasing potentials. The formation of a protein backbone's hydrogen bonds leads to a distinct orientation of dipoles in various types of secondary structures. A balance between charge interactions, hydrogen bonding, and hydrophobicity is responsible for the formation of stable native protein folds. Multiple studies suggest that the ability of proteins and peptides to form amyloid fibril structures is not limited to disease conditions, but a generic property of all polypeptides. The most commonly recognized ß-sheet fibrillar material is an amyloid-like structure, which is linked to a number of diseases from Alzheimer's to diabetes.
