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Inhibitory mechanisms and interaction of tangeretin, 5-demethyltangeretin, nobiletin, and 5-demethylnobiletin from citrus peels on pancreatic lipase: Kinetics, spectroscopies, and molecular dynamics simulation.
Int J Biol Macromol. 2020 Dec 01; 164:1927-1938.IJ

Abstract

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 μM) 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.

Authors+Show Affiliations

School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, People's Republic of China; State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, People's Republic of China.College of Food Science and Engineering, Qingdao Agricultural University, Qingdao 266109, People's Republic of China.School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, People's Republic of China; State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, People's Republic of China.School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, People's Republic of China; State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, People's Republic of China.School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, People's Republic of China; State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, People's Republic of China.School of Perfume and Aroma Technology, Shanghai Institute of Technology, Shanghai 201418, People's Republic of China. Electronic address: arekouxr@sit.edu.cn.School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, People's Republic of China; State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, People's Republic of China. Electronic address: hxwang@jiangnan.edu.cn.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

32795575

Citation

Huang, Xin, et al. "Inhibitory Mechanisms and Interaction of Tangeretin, 5-demethyltangeretin, Nobiletin, and 5-demethylnobiletin From Citrus Peels On Pancreatic Lipase: Kinetics, Spectroscopies, and Molecular Dynamics Simulation." International Journal of Biological Macromolecules, vol. 164, 2020, pp. 1927-1938.
Huang X, Zhu J, Wang L, et al. Inhibitory mechanisms and interaction of tangeretin, 5-demethyltangeretin, nobiletin, and 5-demethylnobiletin from citrus peels on pancreatic lipase: Kinetics, spectroscopies, and molecular dynamics simulation. Int J Biol Macromol. 2020;164:1927-1938.
Huang, X., Zhu, J., Wang, L., Jing, H., Ma, C., Kou, X., & Wang, H. (2020). Inhibitory mechanisms and interaction of tangeretin, 5-demethyltangeretin, nobiletin, and 5-demethylnobiletin from citrus peels on pancreatic lipase: Kinetics, spectroscopies, and molecular dynamics simulation. International Journal of Biological Macromolecules, 164, 1927-1938. https://doi.org/10.1016/j.ijbiomac.2020.07.305
Huang X, et al. Inhibitory Mechanisms and Interaction of Tangeretin, 5-demethyltangeretin, Nobiletin, and 5-demethylnobiletin From Citrus Peels On Pancreatic Lipase: Kinetics, Spectroscopies, and Molecular Dynamics Simulation. Int J Biol Macromol. 2020 Dec 1;164:1927-1938. PubMed PMID: 32795575.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Inhibitory mechanisms and interaction of tangeretin, 5-demethyltangeretin, nobiletin, and 5-demethylnobiletin from citrus peels on pancreatic lipase: Kinetics, spectroscopies, and molecular dynamics simulation. AU - Huang,Xin, AU - Zhu,Junxiang, AU - Wang,Li, AU - Jing,Huijuan, AU - Ma,Chaoyang, AU - Kou,Xingran, AU - Wang,Hongxin, Y1 - 2020/08/11/ PY - 2020/04/25/received PY - 2020/07/11/revised PY - 2020/07/29/accepted PY - 2020/8/17/pubmed PY - 2021/4/7/medline PY - 2020/8/16/entrez KW - Inhibition mechanism KW - Lipase inhibition KW - Molecular dynamics KW - Polymethoxylated flavones SP - 1927 EP - 1938 JF - International journal of biological macromolecules JO - Int J Biol Macromol VL - 164 N2 - 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 μM) 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. SN - 1879-0003 UR - https://www.unboundmedicine.com/medline/citation/32795575/Inhibitory_mechanisms_and_interaction_of_tangeretin_5_demethyltangeretin_nobiletin_and_5_demethylnobiletin_from_citrus_peels_on_pancreatic_lipase:_Kinetics_spectroscopies_and_molecular_dynamics_simulation_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0141-8130(20)34064-2 DB - PRIME DP - Unbound Medicine ER -