1.

Investigation of binding of novel MurD ligands using the ligand-observed NMR methods.

The investigation of interaction of novel MurD inhibitors with the enzyme was presented. We were focused on the NMR methods, which do not require isotope enrichment of the protein. These methods are based on the observation of ligand signals. We used differential line broadening, longitudinal relaxation time and saturation transfere difference (STD) experiments to determine the ligand dissociation constants (KD). A nonlinear regression analysis was applied to extract the KD values from the NMR parameters. Our results indicate that the most accurate KD values are obtained by the STD method.

B.03 Paper at an international scientific conference

COBISS.SI-ID: 3954202

2.

NMR spectroscopy of MurD complexes with novel inhibitors

We implemented the NMR methodology for the identification of binding and for the determination of binding interactions of novel MurD ligands with moderate binding affinity, which were synthesized in Lek pharmaceuticals d.d..

F.17 Transfer of existing technologies, know-how, methods and procedures into practice