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Int J Biol Macromol. 2018 Nov;119:741-746. doi: 10.1016/j.ijbiomac.2018.08.001. Epub 2018 Aug 1.

Antidiabetic and antiparasitic potentials: Inhibition effects of some natural antioxidant compounds on α-glycosidase, α-amylase and human glutathione S-transferase enzymes.

Author information

1
Department of Chemistry, Faculty of Science, Ataturk University, 25240 Erzurum, Turkey.
2
Department of Chemistry, Faculty of Science, Ataturk University, 25240 Erzurum, Turkey. Electronic address: parham_taslimi_un@yahoo.com.
3
Sen Research Group, Department of Biochemistry, Faculty of Arts and Science, Dumlupınar University, Evliya Çelebi Campus, 43100 Kütahya, Turkey.
4
Health Services Vocational School, Igdır University, 76000 Igdır, Turkey.
5
Sen Research Group, Department of Biochemistry, Faculty of Arts and Science, Dumlupınar University, Evliya Çelebi Campus, 43100 Kütahya, Turkey. Electronic address: fatih.sen@dpu.edu.tr.

Abstract

The glutathione S-transferase (GST) was purified from fresh blood erythrocytes using affinity column chromatography. Also, α-amylase from porcine pancreas and α-glycosidase from Saccharomyces cerevisiae were used as target enzymes. In this study, these compounds were tested on α-amylase, α-glycosidase, and GST enzymes and demonstrated effective inhibitor compounds with Ki values in the range of 8.34-40.78 μM against GST, and 120.53-892.36 nM against α-glycosidase. Additionally, the phenolic molecules were tested for the inhibition of α-amylase enzyme which determined effective inhibition profile with IC50 values in the range of 175.01-626.58 nM. Indeed, these molecules can be elective inhibitors of GST, α-glycosidase and α-amylase enzymes as antidiabetic and antiparasitic agents.

KEYWORDS:

Antidiabetic; Antiparasitic; Enzyme inhibition; Glutathione S-transferase

PMID:
30076927
DOI:
10.1016/j.ijbiomac.2018.08.001
[Indexed for MEDLINE]

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