Physics Dept. Seminar
September 19, Monday
Amyloid beta-protein folding and oligomer formation: Molecular dynamics perspective
Prof. Brigita Urbanc
(Biological Physics, Host: Dias)
Room: ECE 202
Time: 11:45 am - 12:45 pm with 11:30 am teatime
Substantial evidence accumulated over several decades implicates soluble oligomers formed by intrinsically disordered amyloid beta-protein (A-beta) as central to Alzheimer's disease pathology. In contrast, a plethora of studies has revealed that A-beta oligomer formation may be an integral part of the normal physiological function of A-beta associated with antiviral and antimicrobial activity in the brain. The exact role of oligomer formation and structural characteristics of the resulting assemblies remain poorly understood. I will elucidate different biophysical approaches aimed at unraveling “structure-function” relationship of A-beta oligomers, with the emphasis on molecular dynamics studies conducted in my group. The overarching aim is to provide insights into novel developments that challenge our notion of A-beta self-assembly as an exclusively pathological process and refine the search for the most proximate A-beta species and/or other circumstances that mediate the onset of the disease.