Event Description
Brigita Urbanc, PhD, Drexel University
Abstract: Aberrant protein aggregation is at the core of many age–triggered diseases, such as Alzheimer’s, Parkinson’s, and Huntington’s disease, amyotrophic lateral sclerosis, type II diabetes, systemic amyloidoses, and others.
These amyloid proteins do not share any obvious aspects of the primary structure yet they self–assemble into cytotoxic low–molecular weight oligomers and form fibrils with a common cross-ß structure. Amyloid ß-protein (Aß) assembly plays a central role in Alzheimer’s disease (AD). I will describe our recent computational and experimental studies that provide insights into oligomer structures of several Aß isoforms and thereby elucidate a possible structural basis of Aß oligomer toxicity. I will also present a minimal model of self–assembly, which reveals unexpected diversity and complexity of assembly pathways and structures characteristic for amyloidogenic proteins and show that a single model parameter can be meaningfully mapped onto the sequence of several amyloidogenic proteins, thus providing a theoretical basis for understanding protein assembly pathways. |
