کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5409001 | 1506534 | 2017 | 68 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Detailed investigation of effects of Zn2Â +, Fe2Â + and Cu2Â + metal ions on the binding interaction between eletriptan hydrochloride an anti-migraine headache drug and bovine serum albumin by various spectrometric techniques and molecular docking studies
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی تئوریک و عملی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Detailed investigation of effects of Zn2Â +, Fe2Â + and Cu2Â + metal ions on the binding interaction between eletriptan hydrochloride an anti-migraine headache drug and bovine serum albumin by various spectrometric techniques and molecular docking studies Detailed investigation of effects of Zn2Â +, Fe2Â + and Cu2Â + metal ions on the binding interaction between eletriptan hydrochloride an anti-migraine headache drug and bovine serum albumin by various spectrometric techniques and molecular docking studies](/preview/png/5409001.png)
چکیده انگلیسی
Bovine serum albumin acts as storage and a transport of endogenous and exogenous compounds with protein in the blood. Eletriptan hydrochloride is an anti-migraine headache drug and binding of this drug to albumin is necessary in pharmacokinetic and pharmacodynamics. Many metal ions are present in blood plasma, therefore, the study on the effects of metal ions on the interaction between drugs and plasma proteins are essential. In this study, the effects of metal ions Zn2 +, Fe2 + and Cu2 + on the interaction between bovine serum albumin (BSA) and eletriptan hydrochloride (ELT) were investigated by employing emission fluorescence, synchronous fluorescence, ultraviolet-visible (UV-Vis) absorption, Fourier transform infrared (FT-IR) spectroscopic and molecular docking studies at physiological buffer conditions (pH 7.4). Results show that static quenching, spontaneous process, hydrogen bonds and vander Waals interactions and the values of Ka, n , Kb, R0 , r and thermodynamic parameters were obtained at different temperatures; then the binding sites for ELT in BSA present in sub-domains IIA, IIIA and IB. The entire outcome indicates that the metal ions decrease the binding efficacy of ELT on BSA. The study of binding phenomena is important in providing basic information on the pharmacological actions, biotransformation and bio-distribution, and this would be useful in pharmaceutical industry, life sciences and clinical medicine.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Liquids - Volume 237, July 2017, Pages 23-37
Journal: Journal of Molecular Liquids - Volume 237, July 2017, Pages 23-37
نویسندگان
Manjushree M, Revanasiddappa Hosakere D.,