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Survey of phytochemical composition and biological effects of three extracts from a wild plant (Cotoneaster nummularia Fisch. et Mey.): A potential source for functional food ingredients and drug formulations
Scopus
Open Access Toplam 120 atıf DOI
This study was focused on the analysis of the phenolic content, antioxidant, antibacterial, anti-cholinesterase, anti-tyrosinase, anti-amylase and anti-glucosidase activity of three solvent extracts from Cotoneaster nummularia. Moreover, water extract was tested in terms of mutagenic/anti-mutagenic effects. The antioxidant activities of these extracts were evaluated by DPPH, ABTS, O2, metal chelating, phosphomolybdenum, b-carotene/linoleic acid, ferric and cupric reducing power assays. Enzyme inhibitory activities were also examined with colorimetric methods. Generally, methanol and water extracts exhibited excellent biological activities. These extracts were rich in phenolic and flavonoid content. Furthermore, Cotoneaster extracts indicated appreciable antibacterial properties against human pathogen strains. HPLC analysis showed that ferulic acid, chlorogenic acid, (-)-epicatechin and (+)-catechin were the major phenolics in extracts tested. These data offer that these extracts from C. nummularia may be considered as a potential source of biological agents for developing functional foods or drug formulations. Copyright:
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In vitro and in silico studies of mangiferin from aphloia theiformis on key enzymes linked to diabetes type 2 and associated complications
Scopus
Havuzumuzda 54 atıf almış
Background: Mangiferin, was identified in the crude methanol extract, ethyl acetate, and n-butanol fractions of Aphloia theiformis (Vahl.) Benn. Objective: This study aimed to analyze the plausible binding modes of mangiferin to key enzymes linked to diabetes type 2 (DT2), obesity, hypertension, Alzheimer's disease, and urolithiasis using molecular docking. Method: Crystallographic structures of α-Amylase, α-glucosidase, glycogen phosphorylase (GP), pancreatic lipase, cholesterol esterase (CEase), angiotensin-I-converting enzyme (ACE), acetyl cholinesterase (AChE), and urease available on the Protein Databank database were docked to mangiferin using Gold 6.0 software. Results: We showed that mangiferin bound to all enzymes by φ-φ and hydrogen bonds mostly. Mangiferin was docked to both allosteric and orthosteric sites of α-glucosidase by φ-φ interactions. However, several hydrogen bonds were observed at the orthosteric position, suggesting a preference for this site. The docking of mangiferin on AChE with the catalytic pocket occupied by paraoxon could be attributed to φ-φ stacking involving amino acid residues, Trp341 and Trp124. Conclusion: This study provided an insight of the molecular interaction of mangiferin with the studied enzymes and can be considered as a valuable tool for designing new drugs for better management of these diseases.
Atıf Yapan Makale Bilgileri
Kurumlar (3)
Selçuk Üniversitesi
Selçuklu, Turkey
University of G. d'Annunzio Chieti and Pescara
Chieti, Italy
University of Mauritius
Reduit, Mauritius