부산대학교 도서관

• Trans -resveratrol binding to lipase CpLIP2 was observed using auto fluorescence of protein. • Enzyme kinetics reveal competitive inhibition between trans -resveratrol and 4-methylumbelliferyl acetate. • Molecular docking results consistent with binding of trans -resveratrol to the active site of lipase CpLIP2. • Quantum-chemical calculations were used to evaluate binding energies. We have examined the trans -resveratrol/lipase interaction by quantitative and qualitative analyses of fluorescence spectra, molecular docking and quantum-chemical calculations at DFT level. Interactions of CpLIP2 from C. parapsilosis CBS 604 and trans -resveratrol were confirmed with a major contribution of tryptophan residues to fluorescence quenching. A thermodynamic study across a wide temperature range was consistent with the presence of a single binding site with a binding free energy of −24 kJ/mol. Nevertheless, trans -resveratrol competitively inhibited CpLIP2 activity. Molecular docking and quantum-chemical calculations were consistent with a strong binding of trans -resveratrol to the CpLIP2 catalytic site via electrostatic and hydrophobic forces. The structural analysis quantitatively revealed an energy transfer from W51 and W350 to trans -resveratrol with a distance of 32 Å. Precise understanding of trans -resveratrol/CpLIP2 interactions has important implications on lipases for screening of stilbenoid. [ABSTRACT FROM AUTHOR]