کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
9890858 1540336 2005 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Binding of the bioactive compound 5,7,4′-trihydroxy-6,3′,5′-trimethoxyflavone to human serum albumin
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Binding of the bioactive compound 5,7,4′-trihydroxy-6,3′,5′-trimethoxyflavone to human serum albumin
چکیده انگلیسی
5,7,4′-trihydroxy-6,3′,5′-trimethoxyflavone is one of the bioactive components isolated from Artemisia plants possessing antitumor therapeutic activities. In this paper, its binding properties and binding sites located on human serum albumin (HSA) have been studied using UV absorption spectroscopy, fluorescence spectroscopy and Fourier transform infrared (FT-IR) spectra. The results of fluorescence titration revealed that 5,7,4′-trihydroxy-6,3′,5′-trimethoxyflavone could strongly quench the intrinsic fluorescence of HSA by static quenching and there was only one class of binding sites on HSA for this drug. The binding constants at four different temperatures (289, 298, 310, and 318 K) were 1.93, 1.56, 1.22, and 0.93 × 105 L mol−1, respectively. The FT-IR spectra evidence showed that the protein secondary structure changed with reduction of α-helices about 27.6% at the drug to protein molar ratio of 3. The thermodynamic functions standard enthalpy change (ΔH0) and standard entropy change (ΔS0) for the reaction were calculated to be −18.70 kJ mol−1 and 36.62 J mol−1 K−1 according to the van't Hoff equation. These results and the molecular modeling study suggested that hydrophobic interaction was the predominant intermolecular force stabilizing the complex, and 5,7,4′-trihydroxy-6,3′,5′-trimethoxyflavone could bind to the site I of HSA (the Warfarin Binding site).
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 37, Issues 1–2, 30 October 2005, Pages 85-91
نویسندگان
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