Interactions between trans-resveratrol and CpLIP2 lipase/acyltransferase: Evidenced by fluorescence and in silico

• Published in: Food chemistry 2020-07, Vol.318, p.126482-126482, Article 126482
• Main Authors: Nguyen, Thi-Nga, Dubreucq, Eric, Perrier, Veronique, Tran, Quang-Hung, Charpentier, Claudine, Charnay, Clarence, Terki, Ferial, Jay-Allemand, Christian, Bidel, Luc P.R.
• Format: Article
• Language: English
• Subjects: Chemical Sciences; DFT; Docking; ETS-NOCV; Fluorescence; Interaction; Lipase; Trans-resveratrol
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2020.126482

•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.