Dr. Roberto Chica
Engineering a ligand-gated ion channel activated by glucose
Ligand-gated ion channels (LGICs) are proteins that bind a substrate and allow transmembrane ion flow. My main objective is to combine machine learning, multi-state design, and directed evolution to create an LGIC activated by glucose that rivals wild-type efficiency. Coupled with research on insulin-secreting cells the goal is to initiate a new solution for diabetic patients
Travelling, Craft Beer, Video Games, Swimming, Bouldering and Rock Climbing.
Dr. Roberto Chica
Using multi-state enzyme design and high-performance computational simulations to enhance the catalytic power of a de novo enzyme.
Development and experimental validation of next-generation enzyme design algorithms.
Designing projects and plugins in Unreal Engine, working out, watching Netflix, listening to and making music.
Greater Toronto Area, Ontario, Canada.
Dre. Joelle Pelletier
Creating new substrates for transglutaminase labelling by protein engineering
Antibody-drug conjugates (ADC) use antibody specificity to direct drugs to their target, for example, cancer cells. This project uses a microbial transglutaminase enzyme (mTG) to conjugate the surface-exposed glutamine residues of antibodies to an amino-payload. The level of reactivity of different glutamine residues varies for unknown reasons, and the only glutamine residue on the surface of the human IgG antibody to react with mTG is hindered by glycosylation, which is essential for antibody stability and solubility. Our objective is to create new reactive sites on the glycosylated antibody by substituting single, surface-exposed residues in the crystallizable fragment (Fc) region with a glutamine, and to then investigate each mutant’s reactivity for conjugation by the mTG enzyme. The mTG-mediated synthesis of glycosylated ADCs could lead to targeted cancer treatments with better efficacy and fewer side effects.
I play the piano, I enjoy crafting, knitting, sewing, etc. I am also a huge geek (Harry Potter, Star Wars, LOTR, etc.)
St-Eustache, Québec, Canada
Dr. Elizabeth Meiering
Rationally altering protein kinetic stability through design of long range intramolecular contacts and N-myristoyltransferase recognition motifs
Kinetic stability is a physical property of proteins that determines their functional lifetime. Using the β-trefoil proteins hisactophilin and ThreeFoil, the Meiering lab determined that long range intramolecular amino acid contacts are a determinant of kinetic stability. We are further investigating the role of long range contacts in protein kinetic stability by designing and characterizing ThreeFoil mutants that contain fewer long range contacts than the extremely stable parent protein. Additionally, we are designing the N-termini of these mutants to accommodate myristoylation, a cotranslational modification that has been shown to influence kinetic stability and folding kinetics.
Going to the gym, growing mushrooms and various other things
Dr. Andrew Woolley
Designing light-switchable affibody inhibitors
Therapeutic developments around many clinically relevant protein signaling networks are currently held back by the incomplete characterization of their interactions. My project is on the engineering of selective light-switchable affibody-based inhibitors targeting key interactions within those complex networks. In creating tools that can dynamically and reversibly inhibit protein signaling, I aim to enable descriptions of the spatiotemporal dynamics in complex protein signaling networks, informing systems-level approaches to clinical developments that will ultimately lead to better therapeutic outcomes.
Tennis, Reading, and Gardening
Mississauga, Ontario, Canada