Angiotensin-converting enzyme inhibitory effects by plant phenolic compounds: a study of structure activity relationships

J Agric Food Chem. 2013 Dec 4;61(48):11832-9. doi: 10.1021/jf404641v. Epub 2013 Nov 21.

Abstract

In this study, 22 phenolic compounds were investigated to inhibit the angiotensin-converting enzyme (ACE). Tannic acid showed the highest activity (IC50 = 230 μM). The IC50 values obtained for phenolic acids and flavonoids ranged between 0.41 and 9.3 mM. QSAR analysis confirmed that the numbers of hydroxyl groups on the benzene ring play an important role for activity of phenolic compounds and that substitution of hydroxyl groups by methoxy groups decreased activity. Docking studies indicated that phenolic acids and flavonoids inhibit ACE via interaction with the zinc ion and this interaction is stabilized by other interactions with amino acids in the active site. Other compounds, such as resveratrol and pyrogallol, may inhibit ACE via interactions with amino acids at the active site, thereby blocking the catalytic activity of ACE. These structure-function relationships are useful for designing new ACE inhibitors and potential blood-pressure-lowering compounds based on phenolic compounds.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Angiotensin-Converting Enzyme Inhibitors / chemistry*
  • Animals
  • Binding Sites
  • Molecular Docking Simulation
  • Peptidyl-Dipeptidase A / chemistry
  • Phenols / chemistry*
  • Plant Extracts / chemistry*
  • Rabbits
  • Structure-Activity Relationship

Substances

  • Angiotensin-Converting Enzyme Inhibitors
  • Phenols
  • Plant Extracts
  • Peptidyl-Dipeptidase A