Alchemilla viridiflora Rothm.: the potent natural inhibitor of angiotensin I-converting enzyme

• Published in: Molecular and cellular biochemistry Vol. 477; no. 7; pp. 1893 - 1903
• Main Authors: Radovic, Jelena, Surucic, Relja, Niketic, Marjan, Kundakovic-Vasovic, Tatjana
• Format: Journal Article
• Language: English
• Published: New York Springer US 01-07-2022; Springer; Springer Nature B.V
• Subjects: Alchemilla; Analysis; Angiotensin; Angiotensin I; Biochemistry; Bioflavonoids; Biological products; Biomedical and Life Sciences; Cardiology; Computer applications; Conversion; Ellagic acid; Enzymes; Flavone glycosides; Flavones; Flavonoids; Glycosides; Hypertension; Life Sciences; Liquid chromatography; Mass spectrometry; Mass spectroscopy; Medical Biochemistry; Methanol; Oncology; Pentose; Peptidyl-dipeptidase A; Plant extracts; Flavonoids; Chemical composition; Ellagitannins; ACE inhibitors; Alchemilla viridiflora
• ISSN: 0300-8177; 1573-4919
• DOI: 10.1007/s11010-022-04410-7

Alchemilla viridiflora
Rothm., Rosaceae is a herbaceous plant widespread in central Greece, Bulgaria, North Macedonia and Serbia with Kosovo. Liquid chromatography-mass spectrometry analysis leads to the identification of 20 compounds in methanol extract, mainly ellagitannins and flavonoid glycosides. Given that various plant extracts have traditionally been used to treat hypertension and that some of the analyzed methanol extract constituents have beneficial cardiovascular effects, we hypothesized that some of these effects are achieved by inhibiting angiotensin I-converting enzyme (ACE). The dose-dependent ACE inhibitory activities of
A. viridiflora
and miquelianin were observed with an IC
50
of 2.51 ± 0.00 µg/mL of
A. viridiflora
extract compared to the IC
50
of 5.4139 ± 0.00 µM for miquelianin. The contribution of the single compounds to the tested activity was further analyzed through the in silico experimental approach. Computational docking results showed that tiliroside, ellagic acid pentose and galloyl-hexahydroxydiphenoyl-glucose exhibited even better binding affinity for the ACE active site than miquelianin, for which ACE activity was confirmed by an in vitro assay.