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人血红蛋白(HHb)和细胞色素c(Cyt c)与生物源氯氧嗪共轭银纳米花的相互作用:光谱学和分子对接方法

Interaction of human hemoglobin (HHb) and cytochrome c (Cyt c) with biogenic chloroxine-conjugated silver nanoflowers: spectroscopic and molecular docking approaches.

作者信息

Shahabadi Nahid, Zendehcheshm Saba

机构信息

Inorganic Chemistry Department, Faculty of Chemistry, Razi University, Kermanshah, Iran.

Medical Biology Research Center (MBRC), Kermanshah University of Medical Sciences, Kermanshah, Iran.

出版信息

J Biomol Struct Dyn. 2022;40(19):8913-8924. doi: 10.1080/07391102.2021.1919555. Epub 2021 Apr 30.

DOI:10.1080/07391102.2021.1919555
PMID:33928842
Abstract

In this research, the biological activity of the antibacterial drug Chloroxine-conjugated biogenic AgNPs (COX-AgNPs) was investigated in simulated physiological conditions (pH = 7.40). Different spectroscopic methods such as UV-visible, fluorescence, and circular dichroism spectroscopic and docking simulation were employed to evaluate the structural changes in the most important blood proteins (human hemoglobin (HHb) and Cytochrome c (Cyt c)) in the presence of COX-AgNPs. The results showed that the COX-AgNPs can bind to HHb and Cyt c and the secondary structure of these proteins remains unchanged, which is crucial in providing insights into the side effects of newly synthesized drugs on their carriers.Communicated by Ramaswamy H. Sarma.

摘要

在本研究中,研究了抗菌药物氯洛辛共轭生物源银纳米颗粒(COX-AgNPs)在模拟生理条件(pH = 7.40)下的生物活性。采用紫外可见光谱、荧光光谱、圆二色光谱等不同光谱方法以及对接模拟,评估了在COX-AgNPs存在下最重要的血液蛋白(人血红蛋白(HHb)和细胞色素c(Cyt c))的结构变化。结果表明,COX-AgNPs可与HHb和Cyt c结合,且这些蛋白质的二级结构保持不变,这对于深入了解新合成药物对其载体的副作用至关重要。由拉马斯瓦米·H·萨尔马传达。

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