Study on the interaction between bovine serum albumin and starch nanoparticles prepared by isoamylolysis and recrystallization

被引:11
作者
Ji, Na [1 ]
Qiu, Chao [1 ]
Li, Xiaojing [1 ]
Xiong, Liu [1 ]
Sun, Qingjie [1 ]
机构
[1] Qingdao Agr Univ, Sch Food Sci & Engn, Qingdao 266109, Shandong, Peoples R China
关键词
Starch nanoparticles; Bovine serum albumin; Interaction; Spectroscopy; GOLD NANOPARTICLES; QUANTUM DOTS; FLUORESCENCE; PROTEIN; MEDIA; ZNS;
D O I
10.1016/j.colsurfb.2015.03.016
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
The current study primarily investigated the interaction of bovine serum albumin (BSA) with starch nanoparticles (SNPs) prepared by isoamylolysis and recrystallization using UV-vis, fluorescence, transmission electron microscopy (TEM), Fourier transform infrared (FTIR) and circular dichroism (CD). The enhanced absorbance observed by UV-vis spectroscopy and decreased intensity of fluorescence spectroscopy suggested that BSA could bind to SNPs and form a BSA-SNP complex. The synchronous fluorescence spectra revealed that the emission maximum,of Tyr residue (at Delta lambda = 15 nm) was red-shifted at the investigated concentrations range, indicating that the conformation of BSA was changed. Quenching parameters showed that the quenching effect of SNPs was static quenching. TEM images showed that the SNPs were surrounded by protein coronae, indicating that nanoparticle-protein complexes had formed. The FTIR and CD characterization indicated that the SNPs induced structural changes in the secondary structure of BSA. (C) 2015 Elsevier B.V. All rights reserved.
引用
收藏
页码:594 / 599
页数:6
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