Effects of albumin-bound nitrosyl iron complex with thiosulfate ligands on lipid peroxidation and activities of mitochondrial enzymes in vitro

被引:9
|
作者
Faingold, I. I. [1 ]
Poletaeva, D. A. [1 ]
Soldatova, Yu. V. [1 ]
Smolina, A. V. [1 ]
Pokidova, O. V. [1 ]
V. Kulikov, A. [1 ]
Sanina, N. A. [1 ,2 ]
Kotelnikova, R. A. [1 ]
机构
[1] RAS, Inst Problems Chem Phys, Chernogolovka, Moscow Region, Russia
[2] Moscow Reg State Univ, Med Chem Res & Educ Ctr, Mytishchy, Moscow Region, Russia
来源
关键词
Nitric oxide; Nitrosyl iron complexes; Albumin; Monoamine oxidase; Cytochrome c oxidase; NO donors; CYTOCHROME-C-OXIDASE; NITRIC-OXIDE; MONOAMINE-OXIDASE; RAT-LIVER; PEROXYNITRITE; CYTOTOXICITY; HEMOGLOBIN; PROTEINS; OXYGEN;
D O I
10.1016/j.niox.2021.10.002
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Nitric oxide (NO) mediates diverse physiological processes in living organisms. Small molecular NO donors usually lack stability and have a short half-life in human tissues, limiting the therapeutic application. The anionic tetranitrosyl iron complex with thiosulfate ligands (TNIC) is one of the most promising NO donors. This study shows that bovine serum albumin (BSA) can effectively stabilize the TNIC complex under aerobic (physiological) conditions, which contributes to its prolonged action as NO donor. Our results demonstrated that TNIC-BSA inhibits formation of TBARS - standard biomarker for the lipid peroxidation induced oxidative stress. Also, it was found that TNIC-BSA inhibits the catalytic activity of mitochondrial membrane-bound enzymes: cytochrome c oxidase and monoamine oxidase A. Together, these results demonstrate that, stabilization of TNIC with BSA opens up the possibility of its practical application in chemotherapy of socially significant diseases.
引用
收藏
页码:46 / 52
页数:7
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