Pharmaqam
Pharmaqam
sbourgault

BOURGAULT, Steve

Professeur,

Email: bourgault.steve@uqam.ca

Site web : http://www.er.uqam.ca/nobel/bipp/index.htm


Thèmes de recherche :

Pharmacologie moléculaire des hormones peptidiques.

Agrégation et amyloidogenèse des polypeptides.

Étude biophysique des polypeptides intrinsèquement désordonnés.

Expertises :

Synthèse peptidique sur phase solide et en solution, marquage (fluorescent ou radioactif) de peptides, chromatographie, évaluation de l’activité biologique, test de survie cellulaire, formation et caractérisation de fibres amyloïdes

Mots Clés :

Chimie peptidique, biophysique, pharmacologie moléculaire, fibres amyloïdes, purification, caractérisation, glycosaminoglycanes, liposomes, peptides photoactivables, expression protéique

Résumé de recherche :

 It is known that the plasticity of the conformational landscape of natively disordered peptides prompts the formation of transient encounter complexes with low specificity binding partners and these interactions ultimately regulate the balance between folding, misfolding and fibrillogenesis, thereof modulating the biological activities and proteotoxicities of polypeptides.

The overarching goal of our research program is to elucidate how the biochemical microenvironment and the molecular interactome influence the structures and functions of intrinsically disordered peptides and to develop, accordingly, innovative peptide-based therapeutics. This research program includes the biophysical characterization of the interactions between an important family of linear and natively unfolded peptide hormones and glycosaminoglycans (GAGs), the lipidic bilayer of the cell membrane and the major components of the extracellular matrix. We also intent to elucidate the common bioactive conformation encrypted in the N-terminal segment of peptidic ligands of class B G protein-coupled receptors by means of a combination of chemical, structural and pharmacological characterization.

We are also designing innovative tools to regulate the conformational ensemble of natively disordered peptides and to monitor their conformational conversion in complex biological environment. Our group also probe how the crowded and heterogeneous cell membrane and extracellular microenvironment catalyzes the aggregation of natively disordered peptides and alters their pathway(s) of amyloidogenesis, using different amyloidogenic polypeptides such as amylin, amyloid beta, calcitonin and glucagon.