Congratulations to Adem H.-Parisien and Jonathan Besna for their Protein Society Travel Awards Grants. The Protein Society Annual Symposium 2022 (PS36) takes place July 7-10, in San Francisco, California.
Welcome to all 4 new interns at the Joelle Pelletier Lab and congratulations to Alexis Bonneau-Burke for his poster presentation prize at the CGCC's 12th annual symposium!
Meet the new faces on the Intern page!
The Joelle Pelletier Lab is happy to welcome two new graduate students: Maxime Saint-Aubin and Megan-Faye Parker (IRSC scholarship recipient).
Read more about their projects in the members column!
Cytochrome P450 Immobilization Strategies [...] was published in ACS catalysis.
Methods of mutagenesis and library creation was published in BioEssays.
Congratulations to Ali for his oral presentation: Cofactor-free biocatalysis flow system of P450 BM3 enzyme immobilization. The event was held at the MIL campus on May 20th.
Congratulations to Stella Cellier-Goetghebeur and Jonathan Besna for first place prizes at the 2022 PROTEO Symposium, held on May 13th.
In collaboration with the research laboratories of Jean-François Masson (U. de Montréal) and Denis Boudreau (U. Laval), the help of organisms such as Instruments Scientifiques Affinité, Héma-Québec as well as many other collaborators, we are currently developing a combined ELISA and SPR (Surface Plasmon Resonance) approach in order to quantify and characterize antibodies against the SARS-CoV-2 virus.
We are participating in a collaborative effort to make clinical biodetection more readily available.
Transglutaminases catalyze protein cross-linking, by bonding an amine (a protein- or peptide-bound lysine) to the terminal amide of a protein- or peptide-bound glutamine. Transglutaminases are increasingly applied to protein-tagging schemes, where various amine-bearing compounds are linked to proteins, providing modified proteins with new properties.
Cytochrome P450s oxidize hydrophobic compounds to increase the body's capacity to eliminate those compounds. The oxidation reactions they catalyze hold great potential for biocatalytic applications. However, there is a need to tailor cytochrome P450s to catalyze specific, industrially-relevant reactions. We are contributing to a joint computational/experimental effort to improve the efficiency of evolution of this class of enzymes.
Dihydrofolate reductases (or Dfrs) are essential in all dividing cells. As a result, they are crucial drug targets in proliferative diseases such as cancer and bacterial infections. We have evolved human Dfr (hDfr) to be highly resistant to the chemotherapy drug methotrexate, as a tool to improve the efficiency of gene therapy.
Bacteria are increasingly acquiring a distinct, inherently drug-resistant Dfr (DfrB1). We have contributed to understand the properties of this enzyme and have discovered its first inhibitors.
β-lactamases cause bacterial resistance to commonly-prescribed antibiotics such as penicillins, cephamycins, and carbapenems. β-lactamases efficiently hydrolyse those antibiotics, inactivating their antibacterial properties. By way of directed evolution, we have determined that these enzymes evolve readily, adapting to new antibiotics. Importantly, these enzymes appear to tolerate important changes in their intrinsic protein motions, with little effect on their catalytic efficiency.
Université de Montréal
Departement of Chemistry
Campus MIL - Room B-6227
Montreal, Qc, Canada, H2V 0B3
Phone: +1 (514) 343-2124
Fax: +1 (514) 343-7586
@ : email@example.com