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He received his doctoral training in Molecular Biophysics at the Moscow Institute of Physics and Technology, a top-ranked School in the former Soviet Union. He developed an active research program in the physical chemistry of nucleic acids at the Institute of Molecular Genetics in Moscow. He received the decree of Doctor of Science (the top scientific degree in the former USSR) for this research. He is currently a professor at Department of Pharmaceutical Sciences, Colleague of Pharmacy, University of Nebraska Medical Center, Omaha, NE. His research is focused on three major areas – (1) structural genomics, (2) molecular mechanisms Alzheimer’s, Parkinson’s and other protein misfolding diseases, and (3) development of technologies for biomedical nanoimaging approaches. He always had a keen interest in new and innovative instrumentation.
Structural genomics: His current interests are centered around chromatin structure and dynamics and DNA recombination and replication. In the chromatin area, they utilize time-lapse AFM to investigate the spontaneous unwrapping of nucleosomes and have proposed a novel model of chromatin dynamics. His recent experiments with the use a revolutionary high-speed AFM are capable of imaging the dynamics of molecules with video rate, and these have yielded new insights into the pathways of chromatin dynamics. The same methodology has been proven itself in the analysis of DNA recombination. They were recently able to observe directly the branch migration of DNA Holliday junction at high resolution and to fully visualize the mechanism of homologous recombination. The availability of new AFM methodology was critical for his studies of interaction of site-specific DNA binding proteins. His current project on the study molecular mechanism of HIV restriction using natural intracellular defense – APOBEC3 DNA deaminases. Thus, he brings a strong belief in the importance of leading-edge innovative instrumentation.
Alzheimer’s, Parkinson’s and other protein misfolding diseases: His second area of interests is linked with understanding the molecular mechanisms of neurodegenerative disorders. Misfolding and aggregation of proteins are widespread phenomena leading to the development of numerous neurodegenerative disorders such as Parkinson’s, Alzheimer’s, and Huntington’s diseases. He developed an approach in which misfolded states are probed with AFM force spectroscopy. Using this approach, they were able to identify misfolded states of the protein and characterize its properties. The major finding is that a misfolding dimer has a extremely long lifetime in comparison with the fast conformational dynamics of monomers usually occurringon the microsecond-nanosecond time scale. The high stability of misfolded dimers is a fundamental finding, suggesting that the formation of dimers leads to the important huge stabilization of the protein misfolded state. Such stabilization dramatically facilitates the aggregation kinetics and thus triggers the entire aggregation process. This conclusion is in line with recent findings on the critical role of dimers in the self-assembly of proteins. Importantly, recent in vivo studies revealed a high toxicity of dimeric forms of amyloid beta. These important findings would not have been possible without the very best instrumentation.
Nanotechnology development: It is an area of constant interest to him, and this activity has always been an integral part of all of my research projects. They developed an entirely novel surface chemistry enabling us to develop one of the most versatile methodologies for AFM imaging. A spin-off from our research has been improvementsin the AFM force spectroscopy methodology. Therearenow rapidly developing and exciting applications of AFM in molecular pharmacology, drug design and other biomedical applications.
|Yuri L Lyubchenko|
|Editorial: J Mol Pharm Org Process Res 2013, 1: e107|
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