Protein-ligand interactions

For a high-throughput study of protein-ligand interactions, a Nanomate Triversa system was purchased to enable us to study larger series of proteins and ligands.
An innovative study was published in a cooperation with Rothamsted Research UK (Hooper et al. 2009 Chem. Commun., Mansourova et al. 2009 Tetrahedron), where ca. 50 ligands and sex pheromone analogues were screened and their interaction with BmPBP1 was elucidated. The binding energy of bombykol and BmPBP1 is very low and experimentally observable only on this unique combination of Nanomate chip system and Synapt HDMS mass spectrometer. This study is currently extended to study point-mutated BmPBP1 and the contribution of individual amino acids towards the ligand binding. A similar study will be performed for other PBPs and GOBPs from insects.