Ursolic Acid Inhibited Cholesterol Esterase and Pancreatic Lipase Activities and Decreased Micellar Cholesterol Solubility In Vitro-Reference-Cited by-同舟云学术

Ursolic Acid Inhibited Cholesterol Esterase and Pancreatic Lipase Activities and Decreased Micellar Cholesterol Solubility In Vitro

Published:2023-12-27 Issue: Volume:2023 Page:1-16
ISSN:1745-4514
Container-title:Journal of Food Biochemistry
language:en
Short-container-title:Journal of Food Biochemistry

Author:

Jiang Wenjing¹,Huang Qun²,Meng Xiangxing¹,Rehman Rizwan-ur³,Qian Kun¹,Yang Xu⁴,Liu Xiaozhi⁵,Chen Jingnan⁶,Zhang Ye¹,Li Jing¹^ORCID,Wang Jilite⁷^ORCID,Guo Qingbin¹^ORCID,Liu Suwen⁸^ORCID,Wang Hao¹^ORCID

Affiliation:

1. State Key Laboratory of Food Nutrition and Safety, Tianjin University of Science and Technology (TUST), Tianjin 300457, China

2. The Key Laboratory of Environmental Pollution Monitoring and Disease Control, Ministry of Education, Guizhou Medical University, Guiyang, Guizhou 550025, China

3. Department of Bioinformatics and Biosciences, Capital University of Science and Technology, Zone V, Kahuta Road, Islamabad, Pakistan

4. National Center of Supervision and Inspection for Processed Food Quality, Tianjin Institute for Food Safety Inspection Technology, Tianjin 300457, China

5. Tianjin Key Laboratory of Epigenetics for Organ Department in Preterm Infants, The Fifth Central Hospital of Tianjin, Tianjin 300450, China

6. College of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, China

7. Department of Agriculture, Hetao College, Bayannur, Inner Mongolia, China

8. College of Food Science and Technology, Hebei Normal University of Science and Technology, Qinhuangdao, Hebei 066004, China

Abstract

Ursolic acid (UA) is a natural triterpene carboxylic acid with an underlying anti-hyperlipidemia effect. This study examined the mechanism of interactions of UA with cholesterol esterase (CEase), pancreatic lipase (PL), and micellar cholesterol solubility in vitro. The half-maximal inhibitory concentration (IC50) of CEase, PL, and micellar cholesterol solubility was determined to be 0.07 ± 0.01 mg/mL, 1.81 ± 0.13 mg/mL, and 1.73 ± 0.08 mg/mL, respectively. Multispectral combination revealed that UA changed the secondary structure and quenched the intrinsic fluorescence by static quenching of the two enzymes. The interactions were exothermic reaction as determined by enthalpy. Furthermore, molecular docking confirmed that UA was bound to amino acids of two enzymes at active site through hydrophobic interaction and van der Waals forces. Molecular dynamics (MD) simulation found that CEase and PL rearranged with UA to form stable complexes. The strong inhibition effect of CEase and PL mediated by UA might provide additional insight into understanding the role of UA in the hypolipidemic effect.

Funder

Guizhou Medical University

Publisher

Hindawi Limited

Subject

Cell Biology,Pharmacology,Food Science,Biophysics

Link

http://downloads.hindawi.com/journals/jfbc/2023/6637700.pdf

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