期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 164, 期 -, 页码 1927-1938出版社
ELSEVIER
DOI: 10.1016/j.ijbiomac.2020.07.305
关键词
Lipase inhibition; Polymethoxylated flavones; Inhibition mechanism; Molecular dynamics
资金
- national food science and engineering first-class discipline construction project [JUFSTR20180204]
- national key research and development plan in the 13th Five-Year [2017YFD0400803]
This study aimed to reveal the interaction and inhibitory mechanisms of tangeretin (TAN), nobiletin (NBT), and their acidic hydroxylated forms, 5-demethyltangeretin (5-DT) and 5-demethylnobiletin (5-DN) on porcine pancreatic lipase (PPL) using spectroscopic techniques and molecular dynamics (MD) simulation. PPL inhibition assay showed that the inhibitory activity of NBT (IC50 value of 3.60 +/- 0.19 mu M) was superior to those of three polymethoxylated flavones (PMFs), indicating it may be related to the methoxy groups at the 3'-position in its molecular structure. Inhibition kinetic analyses demonstrated that the inhibition types of the 4 PMFs were consistent with the mixed inhibition model, which agreed well with the results from the ultraviolet-visible (UV-Vis) spectroscopy, Circular dichroism (CD), fluorescence spectroscopy, molecular docking, and MD simulation that PMFs could bind to the PPL catalytic site and non-catalytic site, affecting the normal spatial conformation of PPL and weakening its ability to decompose the substrate. All these findings suggest that PMFs are a kind of natural lipase inhibitors, and NBT has the potential as a lipase inhibition precursor because of its unique flavone skeleton structure. (C) 2020 Elsevier B.V. All rights reserved.
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