Noémie-Manuelle Dorval-Courchesne

Noémie-Manuelle Dorval Courchesne is an Associate Professor of Chemical Engineering at McGill University and a Canada Research Chair in Biologically-Derived Materials. She obtained her PhD in Chemical Engineering from MIT in 2015 and then worked as a postdoctoral fellow at the Wyss Institute for Biologically Inspired Engineering at Harvard, before joining McGill in 2017. She was trained as a multidisciplinary scientist and engineer, with a background in biochemistry and chemical engineering. In her research, she integrates synthetic biology with scalable assembly processes, to fabricate functional materials. Her group uses these tools to address sustainability and biomedical challenges through biofabrication. Specifically, her team engineers recombinant self-assembling proteins to fabricate biocomposites for a range of applications, including bioelectronics, bioplastics and responsive textiles.

Prof. Dorval Courchesne is actively involved in industrially-relevant research, with the goal of introducing biologically-derived technologies in real-world products. Among other projects, she has collaborated with Lululemon Athletica Inc on responsive bio-functional fabrics. She is also part of an NSERC CREATE on Sustainable Electronics and Eco-Design (SEED). In addition, Prof. Dorval Courchesne is a member of several research networks on the topics of (bio)materials, (bio)polymers and biotechnology. In 2020, she was recognized as the recipient of a “Christophe Pierre Award for Research Excellence (Early Career)” in the Faculty of Engineering at McGill, and as an “Emerging Leader in Chemical Engineering” by the Canadian Society for Chemical Engineering. In 2021, she became Canada Research Chair, and in 2022, she received a Johnson & Johnson WiSTEM2D Scholars Award.

How to build materials with self-assembling proteins

Protein-based materials represent sustainable and easily customizable alternatives to conventional synthetic polymers. With their biocompatibility, bioactivity and genetic tunability, proteins can be customized for a range of applications. Specifically, protein materials that self-assemble into macromolecular structures and can be produced at large scale are of interest for deployment into wearable devices, tissue scaffolds, and alternatives for commodity materials like plastics, textiles and electronics. Curli fibers and their secretion pathway from Escherichia coli bacteria represent a very promising platform for the secretion and assembly of functional proteins. Once secreted by bacteria cells, CsgA subunits, the self-assembling repeats of curli fibers, form fibrous structures that can further aggregate and gel into macroscopic materials. CsgA can also be genetically customized to confer it a variety of functions.

In this talk, I will describe how my group has engineered functional curli fibers for a range of applications, including functional textiles and plastic-like thin films. I will also present how we have repurposed the curli secretion pathway to secrete other recombinant fusion proteins.and how we have repurposed the curli secretion pathway to secrete other recombinant fusion proteins. For instance, I will highlight our recent advances in expressing and secreting recombinant bacterial collagen in a curli-inspired manner. Utilizing only the essential genes from the curli operon, we have established protocols to extracellularly produce collagen-like proteins that can assemble in triple helical structures. We have further developed simple processes to isolate these biomacromolecules from large volumes of bacterial cultures in a cost-efficient manner with potential for scale-up. We have used both curli fiber and bacterial collagen templates for the biomineralization of inorganic nanomaterials and for the fabrication of protein gels. Such recombinant materials have the potential for further genetic customization, making them promising candidates for a range of multifunctional bio-derived devices.

Noémie-Manuelle Dorval-Courchesne

Christian R Landry

Dr Landry obtained his BSc and MSc degrees from Université Laval (1995-2000). He trained as a PhD student at Harvard University (2001-2006) where he worked on the evolution of gene expression networks. He did a postdoctoral internship on the organization and evolution of protein interaction networks at Université de Montréal (2007-2009). Since 2009, he has been an independent investigator at Université Laval and now holds the CIHR Canada Research Chair in Cellular Systems and Synthetic Biology. He was elected in the inaugural cohort of the College of the Royal Society of Canada, he received the NSERC EWR Steacie Memorial Award for early career researchers in 2017 and the SMBE Mid-career award for outstanding contributions in 2020. In 2021, he received the Université Laval Excellence prize for teaching and mentoring to graduate students and postdocs. In 2024, he was awarded the Canada Gairdner Momentum Award for exceptional scientific research contributions with continued potential for impact on human health.

Evolution of protein networks by gene duplication: complexity without benefits

Gene duplication impacts the evolution of genomes in many ways. One consequence is the addition of connections among proteins in protein interaction networks. Although many of these new connections are most likely contributing novel and advantageous functions to the cell, some could also represent the accumulation of mutations that have led to the neutral evolutionary constructions of molecular complexes. I will present our work done over the past seven years trying to understand this phenomenon through multidisciplinary approaches.

Christian R Landry
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