کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5399235 | 1392675 | 2016 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Interaction of tea polyphenols with serum albumins: A fluorescence spectroscopic analysis
ترجمه فارسی عنوان
تعامل پلی فنول چای با آلبومین های سرم: تجزیه و تحلیل طیفی فلورسانس
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کلمات کلیدی
ITCepicatechin-3-gallateepicatechinepigallocatechinEpigallocatechin-3-gallateEGCEGCGHSABSA - BSAhuman serum albumin - آلبومین سرم انسانیbovine serum albumin - آلبومین سرم گاوECG - الکتروکاردیوگرام یا نوار قلبBinding constant - ثابت اتصالStatic quenching - خنک کننده استاتیکcircular dichroism - رنگ تابی دورانیFluorescence - فلورسنسSerum proteins - پروتئین سرمTea polyphenols - پلی فنل چایCatechin - کاتچین، کتیچینIsothermal titration calorimetry - کالری سنجی تیتاسیون ایزوترمال
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی تئوریک و عملی
چکیده انگلیسی
Interactions of some tea polyphenols, namely (â) Catechin (C), (â)-epicatechin (EC), (-) epicatechin-3-gallate (ECG), (â)-epigallocatechin (EGC) and (â)-epigallocatechin-3-gallate (EGCG) are outlined with the serum albumin proteins. These interactions had all resulted in binding with the proteins with a concomitant static quenching of the protein fluorescence. A fluorescence technique has been considered as the tool to comprehend the polyphenol-protein interactions mainly and simultaneously other spectroscopic techniques used to verify the results have been discussed. In this mini review the different types of equations usually employed to calculate the binding constant values have been outlined, namely, modified Stern Volmer plot, Scatchard plot and Lineweaver Burk equation, with their corresponding results. The n values (number of binding sites) had always been close to unity suggesting a 1:1 complexation with the polyphenols and the protein. A structural change in the polyphenols has been found to alter the binding constant value and the galloyl moiety attached to the C ring of the polyphenols have been found to play a crucial role in this regard. It has been found that an increase in galloyl moiety increases binding of the catechins with proteins.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Luminescence - Volume 169, Part A, January 2016, Pages 220-226
Journal: Journal of Luminescence - Volume 169, Part A, January 2016, Pages 220-226
نویسندگان
Adity Bose,