AI Article Synopsis
- The study investigates the interaction between trans-resveratrol and the enzyme lipase (CpLIP2) using various analytical methods, revealing that tryptophan residues play a key role in fluorescence quenching.
- A thermodynamic analysis indicates a single binding site for trans-resveratrol with a binding free energy of -24 kJ/mol, while also showing that it inhibits lipase activity competitively.
- Molecular docking and quantum-chemical calculations demonstrate a strong binding affinity of trans-resveratrol to the catalytic site of CpLIP2, highlighting significant electrostatic and hydrophobic interactions that could aid in the screening of similar compounds.
Article 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.
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| http://dx.doi.org/10.1016/j.foodchem.2020.126482 | DOI Listing |
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Interactions between trans-resveratrol and CpLIP2 lipase/acyltransferase: Evidenced by fluorescence and in silico.
Food Chem
July 2020
UMR AGAP, University of Montpellier, CIRAD, INRAE, Montpellier SupAgro, F-34060 Montpellier, France. Electronic address:
Article Synopsis
- The study investigates the interaction between trans-resveratrol and the enzyme lipase (CpLIP2) using various analytical methods, revealing that tryptophan residues play a key role in fluorescence quenching.
- A thermodynamic analysis indicates a single binding site for trans-resveratrol with a binding free energy of -24 kJ/mol, while also showing that it inhibits lipase activity competitively.
- Molecular docking and quantum-chemical calculations demonstrate a strong binding affinity of trans-resveratrol to the catalytic site of CpLIP2, highlighting significant electrostatic and hydrophobic interactions that could aid in the screening of similar compounds.
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