SARS-CoV-2 ORF10蛋白及其水溶性金属酞菁配合物的DSC研究

IF 1 4区 化学 Q4 CHEMISTRY, MULTIDISCIPLINARY Macroheterocycles Pub Date : 2023-01-01 DOI:10.6060/mhc224858g
O. I. Koifman, S. S. Guseinov, N. Lebedeva, E. S. Yurina, M. O. Koifman, Y. Gubarev
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引用次数: 0

摘要

对SARS-CoV-2 ORF10蛋白与硫代钴(II)和铜(II)酞菁的相互作用进行了理论和实验研究。通过分子对接方法得到了金属酞菁与ORF10蛋白最可能的配合物结构。钴(II)四硫酞菁以单体状态与蛋白质结合,而forf1 0与铜(II)四硫酞菁的相互作用导致形成的蛋白质复合物聚集,这是通过紫外可见光谱显示的。用差示扫描量热法研究了ORF10蛋白及其与金属酞菁配合物的热变性。对光谱和热化学数据的联合分析使得对ORF10蛋白热变性机理的描述成为可能。
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DSC study of SARS-CoV-2 ORF10 protein and its complexes with water-soluble metal phthalocyanines
A theoretical and experimental study of the interaction of the SARS-CoV-2 ORF10 protein with sulfosubstituted cobalt(II) and copper(II) phthalocyanines was carried out. The structures of the most probable complexes of metal phthalocyanines with the ORF10 protein were obtained by molecular docking methods. Cobalt(II) tetrasulfophthal ocyanine binds to the protein in the monomeric state, while the interaction ofORF1 0 with copper(II) tetrasulfophthalocyanine causes aggregation of the formed protein complexes, which was shown by the UV-Vis spectroscopy. Thermal denaturation of the ORF10 protein and its complexes with metal phthalocyanines was studied by differential scanning calorimetry. A joint analysis of the spectral and thermochemical data made it possible to propose a description of the mechanism of thermal denaturation ofthe ORF10 protein.
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来源期刊
Macroheterocycles
Macroheterocycles CHEMISTRY, MULTIDISCIPLINARY-
CiteScore
2.30
自引率
21.40%
发文量
0
期刊介绍: The journal is a forum for the specialists investigating macroheterocyclic compounds. It publishes original experimental and theoretical works (full papers and short communications) and reviews on synthesis, structural characterization, physical and coordination chemistry as well as practical application of macroheterocycles.
期刊最新文献
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