Natallia Strushkevich

Natallia Strushkevich is an Assistant Professor at Skolkovo Institute of Science and Technology (Skoltech), where she leads a research group at the Center for Molecular and Cellular Biology. Her work focuses on understanding redox-active proteins in humans and mycobacteria, with particular emphasis on the cytochrome P450 (CYP) enzyme family and their role in drug metabolism and tuberculosis pathogenesis.

Dr. Strushkevich's research program investigates how CYP enzymes function in both human drug metabolism and in Mycobacterium tuberculosis. Her laboratory employs complex structural and functional studies to identify natural substrates and develop selective inhibitors of CYP enzymes. In humans, these enzymes metabolize endogenous compounds and drugs while catalyzing critical reactions in cholesterol, vitamin D3, eicosanoids, and steroid hormone biosynthesis. For M. tuberculosis, most CYP functions remain unknown, presenting significant research opportunities for novel tuberculosis treatments.

Analysis of Dr. Strushkevich's recent publications reveals a strong methodological focus on X-ray crystallography combined with biochemical and electrochemical techniques. Her work spans structural biology of redox complexes, ligand binding dynamics, and substrate specificity studies, with particular emphasis on how experimental conditions (like glycerol presence) affect structural interpretations crucial for drug design.

Dr. Strushkevich's research is supported by multiple grants from Russian funding agencies including the Ministry of Science and Higher Education of the Russian Federation (projects 075-00337-20-03 and 075-15-2021-1354), the Russian Foundation for Basic Research (project 122030100168-2), and Moscow Institute of Physics and Technology (project 075-15-2021-684). Her collaborative work involves researchers across multiple institutions specializing in structural biology and mycobacterial research.

Dr. Strushkevich leads a multidisciplinary research group that combines X-ray crystallography, biochemical assays, electrochemical characterization, and molecular dynamics simulations to study protein structure-function relationships in redox systems. Her work on CYP-ferredoxin complexes and ligand binding mechanisms provides critical insights for developing new antitubercular drugs targeting these essential bacterial enzymes.