首页 | 本学科首页   官方微博 | 高级检索  
     检索      


Study on the interaction between oxolinic acid aggregates and protein and its analytical application
Authors:Wu Xia  Zheng Jinhua  Ding Honghong  Ran Dehuan  Xu Wei  Song Yuanyuan  Yang Jinghe
Institution:Key Laboratory of Colloid and Interface Chemistry (Shandong University), Ministry of Education, School of Chemistry and Chemical Engineering, Shandong University, Jinan 250100, Shandong, PR China
Abstract:It was found that oxolinic acid (OA) at high concentration can self-assemble into nano- to micro- meter scale OA aggregates in Tris-HCl (pH 7.48) buffer solution. The nanoparticles of OA were adopted as fluorescence probes in the quantitative analysis of proteins. Under optimum conditions, the fluorescence quenching extent of nanometer scale OA aggregates was in proportion to the concentration of albumins in the range of 3.0 × 10−8 to 3.0 × 10−5 g mL−1 for bovine serum albumin (BSA) and 8.0 × 10−8 to 8.0 × 10−6 g mL−1 for human serum albumin (HSA). The detection limits (S/N = 3) were 3.4 × 10−9 g mL−1 for BSA, and 2.6 × 10−8 g mL−1 for HSA, respectively. Samples were satisfactorily determined. The interaction mechanism of the system was studied using fluorescence, UV-vis, resonance light scattering (RLS) and transmission electron microscope (TEM) technology, etc., indicating that the nonluminescent complex was formed between serum albumin molecular and OA, to disaggregate the self-association of OA, which resulted in the dominated static fluorescence quenching in the system.
Keywords:Fluorescence quenching  Oxolinic acid aggregates  Protein  Interaction study
本文献已被 ScienceDirect PubMed 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号