赵 刚1，杨 丹1，何 茜1，黄曦瑶1，罗 勇2
（1.渤海大学化学与材料工程学院，辽宁锦州 121013；2.青岛市生态环境局胶州分局，山东青岛 266300）
摘要：采用多种光谱法研究了亚甲基蓝（MB）及其代谢产物天青B（AZB）与牛血清白蛋白（BSA）之间的共同作用机制。实验结果表明，MB和AZB对BSA的荧光猝灭均为静态猝灭。298 K时MB和AZB与BSA的结合常数分别为1.71×105 L/mol和8.83×104 L/mol。由熵和焓推断，MB和AZB与BSA的作用力类型均主要为静电作用。位点竞争实验结果表明MB和AZB均结合在BSA的SiteⅠ。紫外-可见吸收光谱法实验结果表明，MB和AZB诱导BSA的构象改变。三者共存时，AZB会与MB竞争结合BSA，减小MB与BSA作用的猝灭常数和结合常数，改变MB与BSA的作用力类型。
关键词：亚甲基蓝；天青B；牛血清白蛋白
中图分类号：Q512.1 文献标识码：A 文章编号：1674-506X（2021）02-0023-0007
Study on the Interaction Mechanisms Between Methylene Blue and Its Metabolites with Bovine Serum Albumin
ZHAO Gang1, YANG Dan1, HE Qian1, HUANG Xi-yao1, LUO Yong2
（1.College of Chemistry and Materials Engineering, Bohai University, Jinzhou Liaoning 121013, China;
2.Qingdao Ecological Environment Bureau Jiaozhou Branch, Qingdao Shandong 266300, China）
Abstract：The binding mechanisms between methylene blue (MB) and its metabolite, azure B (AZB), with bovine serum albumin (BSA) were investigated by multi-spectroscopy. The results indicated that the quenching of BSA by MB/AZB were static quenching. The binding constants of MB and AZB with BSA were 1.71×105L/mol and 8.83×104 L/mol at 298 K, respectively. Thermodynamic parameters showed that the binding force of MB/AZB with BSA was electrostatic force. The results of site competition experiments showed that MB and AZB bond to Site Ⅰof BSA. The results of UV-vis spectroscopy showed the conformational changes of BSA upon MB or AZB binding. AZB competed with MB to bind BSA, which reduced the quenching constant and binding constant and changed the binding force of MB with BSA.
Keywords：methylene blue; azure B; bovine serum albumin
doi：10.3969/j.issn.1674-506X.2021.02-003
收稿日期：2020-08-20
基金项目：国家自然科学基金（21676028）
作者简介：赵刚（1979-），男，博士，讲师。研究方向：分析化学。
引文格式：赵刚,杨丹,何茜,等.亚甲基蓝及其代谢产物与牛血清白蛋白相互作用的研究[J].食品与发酵科技,2021,57(2):23-29.
