Journal
FOOD CHEMISTRY
Volume 382, Issue -, Pages -Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2022.132106
Keywords
Lipase; Neochlorogenic acid; Cryptochlorogenic acid; Interaction mechanism; Molecular dynamics simulation
Funding
- National Natural Science Foundation of China [31772047]
- Fundamental Research Funds for the Central Universities of China [2662019PY031]
- National Key R&D Program of China [2019YFC1606003]
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Polyphenols, specifically chlorogenic acid isomers, have inhibitory effects on lipase. The study found that neochlorogenic acid had better inhibitory effect than cryptochlorogenic acid, and electrostatic interaction force played a major role in the lipase-cryptochlorogenic acid system. Molecular dynamics studies showed that neochlorogenic acid had a greater impact on the lipase structure.
Polyphenols are inhibitors for lipase, but the binding selectivity and mechanism of polyphenol isomers and how they interact with lipase are not clear. Here, chlorogenic acid (CGA) isomers, neochlorogenic acid (NCGA) and cryptochlorogenic acid (CCGA) were used to explore the binding selectivity and mechanism of lipase. An inhibition assay indicated that both CGA isomers had dose-dependent inhibitory effects on lipase; however, the inhibitory effect of NCGA was better (IC50: 0.647 mg/mL) than that of CCGA (IC50: 0.677 mg/mL). NCGA and CCGA formed complexes with lipase at a molar ratio of 1:1, and the electrostatic interaction force plays a major role in the lipase-CCGA system. Molecular dynamics studies demonstrated that NCGA had a greater impact on the structure of lipase. The multi-spectroscopic and modeling results explained the effects of micro-structural changes on the binding site, the interaction force and the inhibition rate of the isomers when they combined with lipase.
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