Professor Nicolas Doucet and his research team at the Institut national de la recherche scientifique (INRS) are investigating the conformational changes in proteins and enzymes and their implications for biological function and evolution. Their recent findings, published in the journal Structure, indicate that while structural similarities exist among homologous enzymes across species, their dynamic motions can diverge significantly. This research suggests that specific protein motions are crucial for maintaining biological function, potentially serving as selective pressures during evolution.
These insights have important therapeutic applications, particularly in drug development for serious diseases like cancer and antibiotic resistance. By understanding the molecular dynamics involved in enzyme function, the team aims to create novel inhibitors that target both active and allosteric sites of enzymes. This approach could enhance the specificity of treatments while minimizing antibiotic resistance, a critical global health issue.
The study focused on ribonucleases (RNases) from various vertebrates, revealing that enzymes with similar functions share dynamic profiles, whereas those with different functions demonstrate unique dynamics. This work paves the way for innovative allosteric inhibitor designs, enabling precise targeting of enzymes without affecting their homologs. Funding for the study was provided by several institutions, including NSERC and NIH.
