NMR study of protein-ligand interaction

My PhD project was focused on the study of protein-ligands interactions using different NMR techniques. NMR has a long history in drug discovery and hit-to-lead optimization. Compared to many other biophysical techniques, NMR has advantage of combining, structural and functional parameters to characterize protein inhibitor interactions. NMR experiments for protein-ligands interactions can be divided into two main categories: protein observed and ligand-observed experiments. Using protein-observed NMR experiments, such as Chemical Shift Mapping, I studied the Gp36-MPER/C8 interaction. The Gp36-MPER/C8 plays an important role in the Felin Immunodeficiency Virus (FIV) membrane fusion process. FIV is a naturally occurring lentivirus that is studied as a model system for anti-HIV vaccines and anti-HIV drug development. We have previously demonstrated that a 8 residues fragment (C8) included the membrane proximal external region MPER of Gp36, is endowed with antiviral activity by inhibiting in the cell virus entrance [edited by author]