کد مقاله کد نشریه سال انتشار مقاله انگلیسی ترجمه فارسی نسخه تمام متن
5399438 1505905 2014 26 صفحه PDF سفارش دهید دانلود رایگان
عنوان انگلیسی مقاله ISI
Interaction mode and nanoparticle formation of bovine serum albumin and anthocyanin in three buffer solutions
ترجمه فارسی عنوان
حالت تعامل و تشکیل نانو ذرات آلبومین سرم گاو و آنتوسیانین در سه محلول بافر
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
سفارش ترجمه تخصصی
با تضمین قیمت و کیفیت
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی تئوریک و عملی
چکیده انگلیسی
Investigation of interaction mode of bovine serum albumin (BSA) and anthocyanin (ACN) in different solutions will help us understand the interaction mechanism and functional change of bioactive small molecule and biomacromolecule. This study investigated the binding mode, including binding constant, number of binding sites, binding force of BSA and ACN interaction in three buffer solutions of phosphate (PBS), sodium chloride (NaCl), and PBS-NaCl, using fluorescence spectroscopy and synchronous fluorescence spectroscopy. Formation and characteristics of BSA-ACN complex were also investigated using dynamic light scattering (DLS) and transmission electron microscopy (TEM). The results showed that ACN could interact with BSA at both tyrosine (Tyr) and tryptophan (Trp) residues through both hydrogen bonds and van der Waals force, and the same binding mode was seen in dH2O and three buffer solutions. The value of binding constant K was decreased as the temperature increased from 298 K to 308 K, and the decreasing degree was in the order of dH2O (9.0×104)>NaCl (2.64×104)/PBS (2.37×104)>PBS-NaCl (0.88×104), which was inversely correlated with the ionic strength of the buffer solutions of PBS-NaCl>NaCl>PBS. It indicated that stability of BSA-ACN complex was affected most in dH2O than in three buffer solutions. The BSA and ACN interaction led to formation of BSA-ACN nanoparticles. The sizes of BSA-ACN nanoparticles in dH2O were smaller than that in three buffer solutions, which correlated with stronger binding force between BSA and ACN in dH2O than in three buffer solutions at room temperature (25 °C, 298 K).
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Luminescence - Volume 155, November 2014, Pages 244-250
نویسندگان
, , , ,
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
سفارش ترجمه تخصصی
با تضمین قیمت و کیفیت