The α-glucosidase inhibitory activity and behavior of taxifolin was first investigated by spectrofluorimetry and molecular docking. It was found that taxifolin inhibits α-glucosidase in a competitive manner with the IC50 value of 0.16 mg/mL. The intrinsic fluorescence quenching of α-glucosidase in the presence of taxifolin was observed by the static quenching mechanism. According to the thermodynamic study, the complex of taxifolin and α-glucosidase was maintained by van der Waals and hydrogen bonding. The binding mode provided by molecular docking simulation indicated the existence of hydrogen bonding between taxifolin and the amino acid residues of α-glucosidase (Glu429, Asp 568 and Glu771), which coincided with the result of fluorescence analysis.
VinerR, WhiteB, ChristieD. (2017) Type 2 diabetes in adolescents: a severe phenotype posing major clinical challenges and public health burden. The Lancet, 389, 2252–2260.
2.
HuangH, YanP, ShanZ, ChenS, LiM, LuoC, GaoH, HaoL, LiuL. (2015) Adverse childhood experiences and risk of type 2 diabetes: A systematic review and meta-analysis. Metabolism, 64, 1408–1418.
3.
GhoshS, RanganL. (2015) Molecular docking and inhibition kinetics of α-glucosidase activity by labdane diterpenes isolated from tora seeds (Alpinia nigra B.L. Burtt.). Applied Biochemistry and Biotechnology, 175, 1477–1489.
4.
ToobaeiZ, YousefiR, PanahiF, ShahidpourS, NourisefatM, DoroodmandMM, Khalafi-NezhadA. (2015) Synthesis of novel poly-hydroxyl functionalized acridine derivatives as inhibitors of α-glucosidase and α-amylase. Carbohydrate Research, 411, 22–32.
5.
HuR, LiY, LvQ, WuT, TongN. (2015) Acarbose monotherapy and type 2 diabetes prevention in eastern and western prediabetes: An ethnicity-specific meta-analysis. Clinical Therapeutics, 37, 1798–1812.
6.
ShenL, SunX, YaoL. (2009) Voglibose for prevention of type 2 diabetes mellitus. The Lancet, 374, 448–449.
7.
Figueiredo-GonzálezM, GrossoC, ValentãoP, AndradePB. (2016) α-Glucosidase and α-amylase inhibitors from Myrcia spp.: a stronger alternative to acarbose?. Journal of Pharmaceutical and Biomedical Analysis, 118, 322–327.
8.
AminudinNI, AhmadF, TaherM, ZulkifliRM. (2015) α-Glucosidase and 15-lipoxygenase inhibitory activities of phytochemicals from Calophyllum symingtonianum. Natural Product Communications, 10, 1585–1587.
9.
ChenH, OuyangK, JiangY, YangZ, HuW, XiongL, WangN, LiuX, WangW.(2017) Constituent analysis of the ethanol extracts of Chimonanthus nitens Oliv. leaves and their inhibitory effect on α-glucosidase activity. International Journal of Biological Macromolecules, 98, 829–836.
10.
KamiyamaO, SanaeF, IkedaK, HigashiY, MinamiY, AsanoN, AdachiI, KatoA. (2010) In vitro inhibition of α-glucosidases and glycogen phosphorylase by catechin gallates in green tea. Food Chemistry, 122, 1061–1066.
11.
WeidmannAE. (2012) Dihydroquercetin: More than just an impurity?European Journal of Pharmacology, 684, 19–26.
SunX, ChenRC, YangZH, SunGB, WangM, MaXJ, YangLJ, SunXB. (2014) Taxifolin prevents diabetic cardiomyopathy in vivo and in vitro by inhibition of oxidative stress and cell apoptosis. Food and Chemical Toxicology, 63, 221–232.
15.
LiYQ, ZhouFC, GaoF, BianJS, ShanF. (2009) Comparative evaluation of quercetin, isoquercetin and rutin as inhibitors of alpha-glucosidase. Journal of Agricultural and Food Chemistry, 57, 11463–11468.
16.
JingJ, QuX, TuZ. (2014) Spectroscopic investigations of the interaction of the anti-hypertension drug valsartan with human serum albumin. Molecular Medicine Reports, 9, 2191–2196.
17.
DolatabadiJ, PanahiazarV, BarzegarA. (2014) Spectroscopic and molecular modeling studies of human serum albumin interaction with propyl gallate. RSC Advances, 4, 64559–64564.
18.
XiaoH, LiuB, MoH, LiangG. (2015) Comparative evaluation of tannic acid inhibiting α-glucosidase. Food Research International, 76, 605–610.
