Exploring the structure–activity relationship and interaction mechanism of flavonoids and α-glucosidase based on experimental analysis and molecular docking studies

Abstract

An integrated method was explored to investigate the structure–activity relationship and interaction mechanism between a library of natural flavonoids and α-glucosidase.

Complexation of curcumin with cyclodextrins adjusts its binding to plasma proteins

“…38 The fluorescence peak of Tyr residues has been reported to exhibit a blueshift from 288 to 287 nm after binding curcumin, which is consistent with a reduction in the polarity of the microenvironment around the Tyr residues. 39 In our study, the addition of HP-β-CD and β-CD did not change the position of the fluorescence peak associated with the Tyr residues, while the addition of SACD shifted the peak from 287 to 288 nm. As reported previously, 40 an unchanged maximum emission peak corresponds to a well-protected conformational protein structure.…”

Cooking and In Vitro Digestion Modulate the Anti-Diabetic Properties of Red-Skinned Onion and Dark Purple Eggplant Phenolic Compounds

“…Moreover, some other investigations generically identified flavonols as the active compounds against α-glucosidase in plant extracts [ 19 ]. Previous structure–activity relationship studies highlighted that the catechol moieties in the A- and B-rings as well as the OH group at the C3 position were of paramount importance for the inhibitory activity of flavonoids against α-glucosidase [ 53 , 54 ]. However, the supposed active compounds identified in in vitro digested red-skinned onion were glycosylated at the C4′ and/or C3 position.…”

Investigation of effective natural inhibitors for starch hydrolysing enzymes from Simaroubaceae plants by molecular docking analysis and comparison with in-vitro studies

“…Also, the additional hydrogen bond interactions were observed between the indole moiety and D68, D214, D349, and R439 ( Figure 15 ). The active site residues of Saccharomyces cerevisiae isomaltase such as D215, 352, and E277 are believed to play a key role as the catalytic residues and, these correspond to D214, D349, and E276 in YAG ( Tang et al., 2020 ). Interestingly, the picrasidine-X showed the hydrogen bond interactions with D214 and D349 making it difficult for the substrate molecules to bind to the YAG active site and thereby hinder the catalytic activity.…”