Lebedeva Natalia Sh, Yurina Elena S, Gubarev Yury A, Koifman Oskar I
G.A. Krestov Institute of Solution Chemistry of the Russian Academy of Sciences, Ivanovo 153045, Russia.
G.A. Krestov Institute of Solution Chemistry of the Russian Academy of Sciences, Ivanovo 153045, Russia.
Spectrochim Acta A Mol Biomol Spectrosc. 2021 Feb 5;246:118975. doi: 10.1016/j.saa.2020.118975. Epub 2020 Sep 23.
In this paper was studied the interaction of deutero- and hematoporphyrin with bovine serum albumin, using various methods of physico-chemical analysis. It was established that the localization of porphyrins occurred in the IB subdomain, while hematoporphyrin interacted with the protein in a monomeric form, and deuteroporphyrin - as a J-dimer. Based on spectral studies, the affinity constants of binding albumin with porphyrins were determined, and the affinity of the protein for deuteroporphyrin appeared to be higher than for hematoporphyrin. It was shown that the interaction of albumin with the studied porphyrins led to a change in the secondary structure of the protein, it being accompanied by a decrease in the proportion of disordered protein fragments and an increase in β-folding.
本文采用多种物理化学分析方法研究了氘代卟啉和血卟啉与牛血清白蛋白的相互作用。结果表明，卟啉定位于IB亚结构域，血卟啉以单体形式与蛋白质相互作用，而氘代卟啉则以J-二聚体形式存在。基于光谱研究，测定了白蛋白与卟啉的结合亲和常数，结果显示蛋白质对氘代卟啉的亲和力高于血卟啉。研究表明，白蛋白与所研究的卟啉相互作用导致蛋白质二级结构发生变化，同时无序蛋白质片段比例降低，β-折叠增加。
