Quercetin and Its Metabolites Inhibit Recombinant Human Angiotensin-Converting Enzyme 2 (ACE2) Activity

Liu X., Raghuvanshi R., Ceylan F. D., Bolling B. W.

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, vol.68, no.47, pp.13982-13989, 2020 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 68 Issue: 47
  • Publication Date: 2020
  • Doi Number: 10.1021/acs.jafc.0c05064
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Analytical Abstracts, Applied Science & Technology Source, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, Biotechnology Research Abstracts, CAB Abstracts, Chemical Abstracts Core, Chimica, Compendex, EMBASE, Environment Index, Food Science & Technology Abstracts, MEDLINE, Pollution Abstracts, Veterinary Science Database, DIALNET
  • Page Numbers: pp.13982-13989
  • Keywords: quercetin, angiotensin-converting enzyme 2, enzyme kinetics, polyphenols, TISSUE DISTRIBUTION, SARS CORONAVIRUS, BLOOD-PRESSURE, RECEPTOR, PEPTIDASE, FAMILIES, HOMOLOG, PLASMA, SITE
  • Istanbul Technical University Affiliated: Yes


Angiotensin-converting enzyme 2 (ACE2) is a host receptor for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Inhibiting the interaction between the envelope spike glycoproteins (S-proteins) of SARS-CoV-2 and ACE2 is a potential antiviral therapeutic approach, but little is known about how dietary compounds interact with ACE2. The objective of this study was to determine if flavonoids and other polyphenols with B-ring 3',4'-hydroxylation inhibit recombinant human (rh)ACE2 activity. rhACE2 activity was assessed with the fluorogenic substrate Mca-APK(Dnp). Polyphenols reduced rhACE2 activity by 1566% at 10 mu M. Rutin, quercetin-3-O-glucoside, tamarixetin, and 3,4-dihydroxyphenylacetic acid inhibited rhACE2 activity by 42- 48%. Quercetin was the most potent rhACE2 inhibitor among the polyphenols tested, with an IC50 of 4.48 mu M. Thus, quercetin, its metabolites, and polyphenols with 3',4'-hydroxylation inhibited rhACE2 activity at physiologically relevant concentrations in vitro.