Discovery of natural anthraquinones as potent inhibitors against pancreatic lipase: structure-activity relationships and inhibitory mechanism

J Enzyme Inhib Med Chem. 2024 Dec;39(1):2398561. doi: 10.1080/14756366.2024.2398561. Epub 2024 Sep 2.

Abstract

Obesity is acknowledged as a significant risk factor for various metabolic diseases, and the inhibition of human pancreatic lipase (hPL) can impede lipid digestion and absorption, thereby offering potential benefits for obesity treatment. Anthraquinones is a kind of natural and synthetic compounds with wide application. In this study, the inhibitory effects of 31 anthraquinones on hPL were evaluated. The data shows that AQ7, AQ26, and AQ27 demonstrated significant inhibitory activity against hPL, and exhibited selectivity towards other known serine hydrolases. Then the structure-activity relationship between anthraquinones and hPL was further analysed. AQ7 was found to be a mixed inhibition of hPL through inhibition kinetics, while AQ26 and AQ27 were effective non-competitive inhibition of hPL. Molecular docking data revealed that AQ7, AQ26, and AQ27 all could associate with the site of hPL. Developing hPL inhibitors for obesity prevention and treatment could be simplified with this novel and promising lead compound.

Keywords: Pancreatic lipase; anthraquinones; inhibitor; structure-activity relationships.

MeSH terms

  • Anthraquinones* / chemical synthesis
  • Anthraquinones* / chemistry
  • Anthraquinones* / pharmacology
  • Biological Products / chemical synthesis
  • Biological Products / chemistry
  • Biological Products / pharmacology
  • Dose-Response Relationship, Drug*
  • Drug Discovery*
  • Enzyme Inhibitors* / chemical synthesis
  • Enzyme Inhibitors* / chemistry
  • Enzyme Inhibitors* / pharmacology
  • Humans
  • Lipase* / antagonists & inhibitors
  • Lipase* / metabolism
  • Molecular Docking Simulation
  • Molecular Structure
  • Pancreas* / enzymology
  • Structure-Activity Relationship

Substances

  • Anthraquinones
  • Lipase
  • Enzyme Inhibitors
  • PNLIP protein, human
  • Biological Products

Grants and funding

This work was financially supported by the National Natural Science Foundation of China (82304611), Basic Research Program of Guizhou Province (ZK[2022]376), Key Laboratory of Basic Pharmacology of Ministry of Education (Zunyi Medical University) (KY[2022]393) and the Science and Technology Foundation of Guizhou Provincial Health Commission (gzwkj2022-088).