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Workshops & seminars

"Probing the molecular pathway of amyloid fibrils formation"
Dr. Steve Bourgault (UQAM)


Date & time
Friday, October 16, 2015
2:30 p.m. – 3:30 p.m.
Speaker(s)

Dr. Steve Bourgault

Cost

This event is free

Website

Contact

Dajana Vuckovic

Where

Richard J. Renaud Science Complex
7141 Sherbrooke W.
Room SP-S110

Wheel chair accessible

Yes

Protein aggregation and amyloid deposition are associated with several diseases, including Alzheimer’s disease, diabetes mellitus type 2 (DM-2) and various systemic amyloidoses. These protein misfolding disorders differ on the identity and nature of the protein that misassembles into aggregates, including those with a cross-β-sheet amyloid structure. Substantial evidence supports the amyloid hypothesis, i.e. that a multi-step process of protein aggregation causes cellular and tissue degeneration. Nonetheless, critical issues regarding the (bio)chemical mechanisms underlying these diseases remain unknown, counteracting the development of targeted therapeutic approaches. For instance, it is not understood why a given protein forms amyloid fibrils in a particular tissue and by which pathways it misfolds into insoluble aggregates. Our group is studying the molecular basis of peptide and protein self-assembly in the context of their interactions with biological factors, including glycosaminoglycans and lipid bilayers. We are focusing on the mechanisms of amyloid formation of two polypeptide precursors; the intrinsically disordered peptidic hormone islet amyloid polypeptide (IAPP), whose aggregation is associated with DM-2, and the variable domain of the immunoglobulin light chain. By means of a combination of (bio)chemical and biophysical approaches, we are probing the roles of structural conversion in the pathway(s) by which these polypeptides self-assemble and trigger cell degeneration. 

Steve Bourgault received his Ph.D. in biology from the INRS-Institut Armand-Frappier and the Université de Rouen (joint doctoral thesis) in 2009. He performed post-doctoral research at the Department of Chemistry of The Scripps Research Institute (2009-12). Since 2012, he is an Assistant Professor at the Department of Chemistry of Université du Québec à Montréal (UQÀM). His research focuses on understanding protein aggregation and peptide hormone molecular pharmacology and on developing chemical and biochemical tools to study polypeptide conformational transition.    

He is the guest of Dr. Peter Pawelek.

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