1403/01/10
محمد حسین فاطمی

محمد حسین فاطمی

مرتبه علمی: استاد
ارکید:
تحصیلات: دکترای تخصصی
اسکاپوس:
دانشکده: دانشکده شیمی
نشانی:
تلفن: 01135342931

مشخصات پژوهش

عنوان
Determination of the binding constant of some synthetic food dyes to human serum albumin using biopartitioning micellar chromatography and molecular docking
نوع پژوهش
Presentation
کلیدواژه‌ها
Synthetic food dyes, Biopartitioning micellar chromatography, Human serum albumin, Chemometrics, Molecular docking
سال
2017
پژوهشگران Mohammad Reza Hadjmohammadi ، Parvin Hoseyni ، Mohammad Hossein Fatemi

چکیده

Due to the high amount of artificial food colorants present in diets, their adverse effects have been of major concern among the literature. Artificial food colorants have been suggested to affect children’s behavior, being hyperactivity the most common disorder[1-3]. Human serum albumin (HSA) is the most important artificial food colorants carrier in humans. Consequently, the study of the interaction of artificial food colorants with HSA is important[4-9]. Biopartitioning micellar chromatography (BMC) is a mode of micellar liquid chromatography that uses micellar mobile phases of Brij35 under adequate experimental conditions(the column temperature was kept at stable 36.5◦C to approach normal human body temperature, The pH of the micellar eluent was adjusted to 7.4 with 0.05 M phosphate buffer, prepared with disodium hydrogenphosphate and sodium dihydrogenphosphate , To reproduce the osmotic pressure of biological fluids, NaCl (9.2 g L−1) was added to the micellar mobile phase.)[10]. However, Mobile phases were prepared by aqueous solutions of 0.01 and0.007 M Brij35 . In this paper, relationships between the BMC retention data of artificial food colorants and binding constant of them are studied and the predictive ability of models is evaluated. Another method is the study of the interaction of the HAS-ligand by molecular docking. Molecular docking is one of the most widely used computing tools. Docking calculations simulate the interaction of an active compound and the active site of a protein. Hence, the results of this study are in good agreement with the results obtained from biochemical studies[11].