ArticleJournal of enzyme inhibition and medicinal chemistry2019
Soyasaponins from Zolfino bean as aldose reductase differential inhibitors.
Article in Journal of enzyme inhibition and medicinal chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- ExploringMolecules (Basel, Switzerland) · 2026Article
- Anti-lipidemic and anti-diabetic properties ofIn silico pharmacology · 2025Article
- Models of enzyme inhibition and apparent dissociation constants from kinetic analysis to study the differential inhibition of aldose reductase.Journal of enzyme inhibition and medicinal chemistry · 2022Article
- Article
- In Search of Differential Inhibitors of Aldose Reductase.Biomolecules · 2022Review
- Intra-site differential inhibition of multi-specific enzymes.Journal of enzyme inhibition and medicinal chemistry · 2020Review
- Aldose Reductase Differential Inhibitors in Green Tea.Biomolecules · 2020Article
- Can Medicinal Plants and Bioactive Compounds Combat Lipid Peroxidation Product 4-HNE-Induced Deleterious Effects?Biomolecules · 2020Review
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Authors and funding
12 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Seven triterpenoid saponins were identified in methanolic extracts of seeds of the Zolfino bean landrace (Phaseolus vulgaris L.) by HPLC fractionation, revealing their ability to inhibit highly purified human recombinant aldose reductase (hAKR1B1). Six of these compounds were associated by MS analysis with the following saponins already reported in different Phaseolus vulgaris varieties: soyasaponin Ba (V), soyasaponin Bb, soyasaponin Bd (sandosaponin A), soyasaponin αg, 3-O-[R-l-rhamnopyranosyl(1 → 2)-α-d-glucopyranosyl(1 → 2)-α-d-glucuronopyranosyl]olean-12-en-22-oxo-3α,-24-diol, and soyasaponin βg. The inhibitory activity of the collected fractions containing the above compounds was tested for hAKR1B1-dependent reduction of both l-idose and 4-hydroxynonenal, revealing that some are able to differentially inhibit the enzyme. The present work also highlights the difficulties in the search for aldose reductase differential inhibitors (ARDIs) in mixtures due to the masking effect on ARDIs exerted by the presence of conventional aldose reductase inhibitors. The possibility of differential inhibition generated by a different inhibitory model of action of molecules on different substrates undergoing transformation is also discussed.
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