M. Babych

Compartmentalized processing of catechols during mussel byssus fabrication determines the destiny of DOPA

Matthew J. Harrington, C. Thibodeaux, S. Bourgault, 2020, Proceedings of the National Academy of Sciences.

Cell surface glycosaminoglycans exacerbate plasma membrane perturbation induced by the islet amyloid polypeptide

S. Bourgault, M. Sebastiao, P. T. Nguyen, 2021, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Site-Specific Alkylation of the Islet Amyloid Polypeptide Accelerates Self-Assembly and Potentiates Perturbation of Lipid Membranes.

M. Golizeh, S. Bourgault, L. Sleno, 2021, Biochemistry.

Harnessing the Activation of Toll-Like Receptor 2/6 by Self-Assembled Cross-β Fibrils to Design Adjuvanted Nanovaccines

S. Bourgault, D. Archambault, Ximena Zottig, 2020, Nanomaterials.

Engineering and evaluation of amyloid assemblies as a nanovaccine against the Chikungunya virus.

S. Bourgault, D. Archambault, G. Bertheau-Mailhot, 2018, Nanoscale.

Contribution of the 12–17 hydrophobic region of islet amyloid polypeptide in self-assembly and cytotoxicity

S. Bourgault, Vy Nguyen, P. T. Nguyen, 2022, Frontiers in Molecular Biosciences.

Identification of a novel TLR5 agonist derived from the P97 protein of Mycoplasma hyopneumoniae.

S. Bourgault, D. Archambault, M. Segura, 2020, Immunobiology.

Guiding the Morphology of Amyloid Assemblies by Electrostatic Capping: from Polymorphic Twisted Fibrils to Uniform Nanorods.

S. Bourgault, D. Archambault, Ximena Zottig, 2019, Small.

Amyloid self‐assembling peptides: Potential applications in nanovaccine engineering and biosensing

S. Bourgault, D. Archambault, Ximena Zottig, 2018, Peptide Science.

Development of a novel fluorescence assay for studying lipid bilayer perturbation induced by amyloidogenic peptides using cell plasma membrane vesicles.

A. Arnold, S. Bourgault, I. Marcotte, 2023, Biochimica et biophysica acta. Biomembranes.

Converting the Amyloidogenic Islet Amyloid Polypeptide into a Potent Nonaggregating Peptide Ligand by Side Chain-to-Side Chain Macrocyclization.

S. Bourgault, P. T. Nguyen, M. Babych, 2024, Journal of the American Chemical Society.