Recently, due to their biological properties, polyphenol-rich functional foods have been proposed to be unique supplementary and nutraceutical treatments for diabetes mellitus. Inhibition of α-amylase and α-glucosidase enzymes using natural products (especially polyphenols) is a novel oral policy to regulate carbohydrate metabolism and hyperglycemia. The present study aims to evaluate the α-amylase and α-glucosidase inhibitory activity of 26 polyphenols using molecular docking and virtual screening studies. The results speculate that among selected compounds caffeic acid, curcumin, cyanidin, daidzein, epicatechin, eridyctiol, ferulic acid, hesperetin, narenginin, pinoresinol, quercetin, resveratrol and syringic acid can significantly inhibit the α-glucosidase enzyme. In addition, catechin, hesperetin, kaempferol, silibinin and pelargonidin are potent α-amylase inhibitors. Therefore the primary structure of polyphenols can change the inhibitory effect versus the α-amylase and α-glucosidase enzymes. Finally, we speculate that consumption of polyphenol-rich functional foods (by considering the best dose of each compound and assessing their possible side effects) in diabetic patients may be useful for regulating carbohydrate metabolism and related disorders. The findings of the current study may also shed light on a way of generating a new class of amylase/glucosidase inhibitors that will discriminately inhibit the on-target enzymes with negligible undesired off-target side effects.
The
spectroelectrochemically generated infrared (IR) and near-infrared
spectra of the homo-bimetallic, hexa-1,3,5-triyn-1,6-diyl-bridged
complex cations [{Cp*(dppe)M}(μ-CCC≡CCC){M(dppe)Cp*}]+ (M = Fe, [1]+; Ru, [2]+) have been analyzed using density functional theory
calculations based on global (BLYP35) and local (LH20t) hybrid functionals.
The differences in the number of IR active ν(CCCCCC)
modes in these complexes are attributed to the distinct electronic
localization of the Fe(II)–Fe(III) mixed-valence cation [1]+ on the IR timescale, as opposed to the delocalized
electronic character of [2]+.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.