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Antidiabetic activity of Pterospermum acerifolium flowers and glucose uptake potential of bioactive fraction in L6 muscle cell lines with its HPLC fingerprint.

Paramaguru R, Mazumder PM, Sasmal D, Jayaprakash V - Biomed Res Int (2014)

Bottom Line: Diabetic animals treated with PAFE2 (30 mg/kg) reduced the levels of fasting blood glucose, significantly (P<0.001) compared to that of diabetic control animals.Histological studies on drug treated groups did not show remarkable positive changes in β-cells.HPLC analysis of PAFE2 reveals the presence of quercetin and apigenin as major constituents and both are inhibiting the glycogen phosphorylase enzyme in molecular modelling studies.

View Article: PubMed Central - PubMed

Affiliation: Department of Pharmaceutical Sciences, Birla Institute of Technology, Mesra, Ranchi, Jharkhand-835215, India.

ABSTRACT
The present study was designed to estimate the detailed antidiabetic activity of Pterospermum acerifolium (L.) Willd flowers. In vitro alpha amylase inhibition study was carried out on 50% ethanol extract of flowers (PAFEE) and its various fractions. The active ethyl acetate fraction (PAFEF) was subfractionated into three subfractions (PAFE1, PAFE2, and PAFE3) and subjected to acute toxicity studies followed by antidiabetic screening in vivo by streptozotocin-nicotinamide induced type II diabetes. Diabetic animals treated with PAFE2 (30 mg/kg) reduced the levels of fasting blood glucose, significantly (P<0.001) compared to that of diabetic control animals. Histological studies on drug treated groups did not show remarkable positive changes in β-cells. PAFE2 showed 32.6±1.93% glucose uptake over control and, in the presence of PI3K inhibitor wortmannin, declined to 13.7±2.51%. HPLC analysis of PAFE2 reveals the presence of quercetin and apigenin as major constituents and both are inhibiting the glycogen phosphorylase enzyme in molecular modelling studies. The study evidenced strongly that the probable glucose lowering mechanism of action of active subfraction PAFE2 is by increasing the glucose uptake in peripheral tissues and by inhibition of gluconeogenesis.

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Hydrogen bond interactions between amino acid residues in the active site pocket of glycogen phosphorylase and (a) quercetin and (b) apigenin.
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fig3: Hydrogen bond interactions between amino acid residues in the active site pocket of glycogen phosphorylase and (a) quercetin and (b) apigenin.

Mentions: To investigate the interaction of quercetin and apigenin, molecular docking simulations of the binding of those molecules with glycogen phosphorylase active site were carried out using Autodock 4.2. From this study we found that quercetin is making eight H-bond interactions with the active site residues Asn 284, Lys 568, Lys 574, Tyr 648, Gly 675, Asn 484, and Val 567 and π electrons of flavone nucleus of quercetin is making π-π stacking interaction with Tyr 648 (Figure 3(a)). The estimated free energy binding of quercetin was found to be −8.27 kcal mol−1 with estimated inhibition constant (Ki) of 0.87 μM. Similarly, apigenin is making three hydrogen bond interactions with the active site residues Glu 88, His 377, and Asn 484 (Figure 3(b)). The estimated free energy binding of apigenin was found to be −8.08 kcal mol−1 with estimated inhibition constant (Ki) of 1.2 μM, which infers clearly that the major constituents of bioactive subfraction can inhibit glycogen phosphorylase enzyme.


Antidiabetic activity of Pterospermum acerifolium flowers and glucose uptake potential of bioactive fraction in L6 muscle cell lines with its HPLC fingerprint.

Paramaguru R, Mazumder PM, Sasmal D, Jayaprakash V - Biomed Res Int (2014)

Hydrogen bond interactions between amino acid residues in the active site pocket of glycogen phosphorylase and (a) quercetin and (b) apigenin.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4221968&req=5

fig3: Hydrogen bond interactions between amino acid residues in the active site pocket of glycogen phosphorylase and (a) quercetin and (b) apigenin.
Mentions: To investigate the interaction of quercetin and apigenin, molecular docking simulations of the binding of those molecules with glycogen phosphorylase active site were carried out using Autodock 4.2. From this study we found that quercetin is making eight H-bond interactions with the active site residues Asn 284, Lys 568, Lys 574, Tyr 648, Gly 675, Asn 484, and Val 567 and π electrons of flavone nucleus of quercetin is making π-π stacking interaction with Tyr 648 (Figure 3(a)). The estimated free energy binding of quercetin was found to be −8.27 kcal mol−1 with estimated inhibition constant (Ki) of 0.87 μM. Similarly, apigenin is making three hydrogen bond interactions with the active site residues Glu 88, His 377, and Asn 484 (Figure 3(b)). The estimated free energy binding of apigenin was found to be −8.08 kcal mol−1 with estimated inhibition constant (Ki) of 1.2 μM, which infers clearly that the major constituents of bioactive subfraction can inhibit glycogen phosphorylase enzyme.

Bottom Line: Diabetic animals treated with PAFE2 (30 mg/kg) reduced the levels of fasting blood glucose, significantly (P<0.001) compared to that of diabetic control animals.Histological studies on drug treated groups did not show remarkable positive changes in β-cells.HPLC analysis of PAFE2 reveals the presence of quercetin and apigenin as major constituents and both are inhibiting the glycogen phosphorylase enzyme in molecular modelling studies.

View Article: PubMed Central - PubMed

Affiliation: Department of Pharmaceutical Sciences, Birla Institute of Technology, Mesra, Ranchi, Jharkhand-835215, India.

ABSTRACT
The present study was designed to estimate the detailed antidiabetic activity of Pterospermum acerifolium (L.) Willd flowers. In vitro alpha amylase inhibition study was carried out on 50% ethanol extract of flowers (PAFEE) and its various fractions. The active ethyl acetate fraction (PAFEF) was subfractionated into three subfractions (PAFE1, PAFE2, and PAFE3) and subjected to acute toxicity studies followed by antidiabetic screening in vivo by streptozotocin-nicotinamide induced type II diabetes. Diabetic animals treated with PAFE2 (30 mg/kg) reduced the levels of fasting blood glucose, significantly (P<0.001) compared to that of diabetic control animals. Histological studies on drug treated groups did not show remarkable positive changes in β-cells. PAFE2 showed 32.6±1.93% glucose uptake over control and, in the presence of PI3K inhibitor wortmannin, declined to 13.7±2.51%. HPLC analysis of PAFE2 reveals the presence of quercetin and apigenin as major constituents and both are inhibiting the glycogen phosphorylase enzyme in molecular modelling studies. The study evidenced strongly that the probable glucose lowering mechanism of action of active subfraction PAFE2 is by increasing the glucose uptake in peripheral tissues and by inhibition of gluconeogenesis.

Show MeSH
Related in: MedlinePlus