Mechanistic study on the inhibition of α‐amylase and α‐glucosidase using the extract of ultrasound‐treated coffee leaves
Trigonelline
Docking (animal)
DOI:
10.1002/jsfa.12890
Publication Date:
2023-07-29T19:19:45Z
AUTHORS (6)
ABSTRACT
Our previous studies have shown that ultrasound-treated γ-aminobutyric acid (GABA)-rich coffee leaves higher angiotensin-I-converting enzyme inhibitory activity than their untreated counterpart. However, whether they antidiabetic remains unknown. In this study, we aimed to investigate the activities of leaf extracts (CLEs) prepared with ultrasound (CLE-U) or without (CLE-NU) pretreatment on α-amylase and α-glucosidase. Subsequently, evaluated binding interaction between CLE-U both enzymes using multi-spectroscopic in silico analyses.Ultrasound increased against α-glucosidase by 21.78% 25.13%, respectively. reversibly inhibits enzymes, competitive inhibition observed for non-competitive The static quenching was primarily driven hydrogen bond van der Waals interactions. α-helices were 1.8% 21.3%, Molecular docking results showed key differential compounds, including mangiferin, 5-caffeoylquinic acid, rutin, trigonelline, GABA, caffeine, glutamate, others, present interacted specific amino residues located at active site (ASP197, GLU233, ASP300). these bioactive components involved residues, such as PHE1289, PRO1329, GLU1397, outside site.Ultrasound-treated are potential anti-diabetic substances, capable preventing diabetes inhibiting α-glucosidase, thus delaying starch digestion. study provides valuable information elucidate possible capacity through activities. © 2023 Society Chemical Industry.
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