The structure and synthesis of the vacuolar H+-ATPase enzymes were studied. Two latest molecular probes, including the electron spin labels and photoactivable labels, were used for the analysis of inhibitor binding to the vacuolar ATPase enzyme. The electron paramagnetic resonance (EPR) spectroscopy studies indicated the incorporation of the inhibitors within membranes. On the other hand, the photoaffinity labeling (PAL) investigation suggested that the members of the V-ATPase inhibitors targeted the transmembrane, proteolipid component of the enzyme.
ASJC Scopus subject areas
- Physical and Theoretical Chemistry
- Organic Chemistry