برهمکنش ساپونین استخراج شده از گیاه Tribulus terrestris بر ساختار پروتئین سرم آلبومین انسانی

Subject Areas : Journal of Medicinal Herbs, "J. Med Herb" (Formerly known as Journal of Herbal Drugs or J. Herb Drug)

آزاده حکمت ¹ , رویا برومند ² , کامبیز لاریجانی ³

1 - گروه زیست شناسی ، واحد علوم و تحقیقات ، دانشگاه آزاد اسلامی ، تهران ، ایران
2 - گروه زیست شناسی ، واحد علوم و تحقیقات ، دانشگاه آزاد اسلامی ، تهران ، ایران
3 - گروه زیست شناسی ، واحد تهران مرکز ، دانشگاه آزاد اسلامی ، تهران ، ایران

Received: 2020-01-15 Accepted : 2020-05-21 Published : 2019-04-21

Keywords: Fluorescence, Tribulus terrestris, Spectroscopy, saponins, Human Serum Albumin (HSA), Förster theory,

Abstract :

Background & Aim:Saponins are well-known secondary metabolites with numerous beneficial pharmacological properties. Since the interactions of drugs with blood constituents, in particular with human serum albumin (HSA) may have a major impact on drug pharmacology, the present study designed to provide a fundamental understanding of the interaction of saponins extracted from Tribulus terrestris (typically utilized in folk medicine) with HSA in detail. Experimental: After extraction and purification of saponins; UV-Vis spectroscopy, fluorescence spectroscopy, and far-UV CD spectroscopy were used to examine the effects of saponins from Tribulus terrestris on HSA. Results: Thin-Layer chromatography confirmed the presence of 3 different saponins. The UV-Vis absorption, fluorescence emission and far-UV CD results displayed that saponinsfrom Tribulus terrestris could form a complex with HSA. The binding constant for the saponins–HSA complex was found to be 13.4×104M-1. The distance r between HSA and Tribulus terrestris saponins was also acquired according to the Förster theory. Recommended applications/industries: Altogether, saponins can bind to HSA and change the secondary and tertiary structure of HSA moderately. The results obtained from this study can help in understanding the pharmacokinetic properties of saponins.

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