Dr. C. Sadasivan has been primarily involved in the identification of drug lead compounds using bioinformatics and computational biology approaches, followed by validation through biophysical techniques. He has contributed to the isolation of several antimicrobial compounds from both natural and synthetic sources and evaluated their inhibitory activity against key microbial proteins such as beta-lactamase and alpha-amylase. In addition, he has identified inhibitors targeting important human proteins, including alpha-thrombin, acetylcholinesterase, phospholipase, fatty acid synthase, and adenosine deaminase. His work has also provided insights into the protein targets of the environmental pollutant bisphenol-A in the human body.
Dr. Sadasivan has extensive expertise in structural biology, particularly in the elucidation of protein and DNA structures using single-crystal X-ray crystallography. As part of his doctoral research, he solved the crystal structures of two hexanucleotides. He has also determined the crystal structure of human alpha-thrombin, an enzyme implicated in myocardial infarction, in complex with the factor XIII activation peptide. His research further includes the study of enzyme hydration and structural stability under varying humidity conditions using both crystallographic and computational approaches. Additionally, he has developed several computational tools in FORTRAN for analyzing protein hydration.
