Effect of surfaces and osmolytes in modulating peptide assembly
Seminar | November 26 | 4-5 p.m. | 120 Latimer Hall
Intrinsically disordered peptides are a special class of proteins that do not fold to a unique three-dimensional shape. These proteins play important roles in the cell, from signaling to serving as structural scaffolds. Under pathological conditions, these proteins are capable of self-assembling into structures that are toxic to the cell, and a number of neurodegenerative diseases, such as Alzheimers disease and Parkinsons disease, are associated with this self-assembly process. In this talk, I will discuss the effect of surfaces and the osmolytes urea and TMAO in regulating the structure and assembly of intrinsically disordered peptides. I will focus on two model systems, the mussel foot protein implicated in underwater adhesion of mussels to rocks, and the Tau peptide implicated in Alzheimers Disease.