Structural Biology of Amyloid Fibrils

Prof. Vijay Kumar is a distinguished faculty member and researcher specializing in Structural biology, Protein chemistry and neurosciences. He holds the position of Professor of the Department of Biotechnology, Anand School of Engineering and Technology, Sharda University, Agra. Prof. Kumar is internationally recognized and ranks among the top 2% of most cited scientists according to the STANFORD list. He earned his PhD in Biophysics from AIIMS, New Delhi, and completed a postdoctoral fellowship at UMass Medical School, focusing on folding and aggregation of proteins such as SOD1 and TDP-43 implicated in motor neuron disease, ALS, and FTD. He also served as Principal Investigator under the DST-SERB Young Scientist Scheme at Jamia Millia Islamia. His current research focuses on protein folding, misfolding, and aggregation, and the role of toxic RNA species in neurodegenerative diseases. He is a member of the Protein Society, Indian Biophysical Society, Indian Academy of Neurosciences, and the International Society for Neurochemistry. He has held fellowships from CSIR, India and a DAAD fellowship in Germany. Prof. O.V. Galzitskaya, Dr. Sci. (Physics and Mathematics), is a leading expert in molecular biology, biophysics, and bioinformatics. She serves as Head of the Bioinformatics Laboratory at the Gamaleya National Research Center (Moscow) and has concurrently headed the Bioinformatics and Proteomics Laboratory at the Institute of Protein Research, RAS, since 2008. Galzitskaya developed the first theory for identifying folding nuclei in protein and RNA structures and elucidated key determinants of protein folding rates. She pioneered a kinetic-based theory for amyloid formation, created the first library of disordered motifs, and developed novel bioinformatics tools for predicting amyloidogenic and natively disordered regions. Her experimental work proposed a new model of amyloid fibril polymorphism and identified a novel target for Alzheimer’s therapeutics. Notably, she discovered a novel case of lysozyme amyloidosis (p.F21L/T88N) in a Russian family and, based on her co-aggregation model, engineered antibacterial peptides effective against Pseudomonas aeruginosa and Staphylococcus aureus.

• 1. Introduction2. SSNMR: Methods and Applications3. Cryo-EM: methods and applications4. Amyloid-beta oligomers and fibrils5. α-Synuclein oligomers and fibrils6. TDP-43 oligomers and fibrils7. Tau oligomers and fibrils8. Prion oligomers and fibrils9. IAPP oligomers and fibrils10. Example and effects of post-translational modifications in amyloid structurePart I11. Effect of post-translational modifications in Amyloid structurePart II12. Chemical modifications and amyloid structure13. Energy landscape of amyloid formation14. Computational studies of amyloid fibrils15. Computational models of amyloid fibrils