Interactions between trans-resveratrol and CpLIP2 lipase/acyltransferase: Evidenced by fluorescence and in silico. (15th July 2020)

• Record Type: Journal Article
• Authors: Nguyen, Thi-Nga; Dubreucq, Eric; Perrier, Veronique; Tran, Quang-Hung; Charpentier, Claudine; Charnay, Clarence; Terki, Ferial; Jay-Allemand, Christian; Bidel, Luc P.R.
• Is Part Of: Food chemistry. Volume 318(2020)
• Publication Date: 2020-07-15
• Subjects: Lipase -- Trans-resveratrol -- Fluorescence -- Interaction -- Docking -- DFT -- ETS-NOCV; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2020.126482
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: 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. Abstract: 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.