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

Faingold, I. I.; Poletaeva, D. A.; Soldatova, Yu. V.; Smolina, A. V.; Pokidova, O. V.; Куликов, А. В.; Санина, Н. А.; Kotelnikova, R. A.

doi:10.1016/j.niox.2021.10.002

Cited by 9 publications

(8 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Quenching of the phosphorescence of eosin Y by TNIC-ThS occurs with bimolecular rate constant 2 × 10 10 M −l s −1 , which is equal to the diffusion-limited Smoluchowski rate. It was previously shown that, in aqueous solutions, TNIC-ThS decomposes into paramagnetic mononuclear dinitrosyl iron complexes, which gradually decay as well [ 45 ]. Thus, the average time an excited eosin Y molecule took to become quenched by TNIC-ThS disintegration products decreased.…”

Section: Resultsmentioning

confidence: 99%

Influence of Nitrosyl Iron Complex with Thiosulfate Ligands on Therapeutically Important Targets Related to Type 2 Diabetes Mellitus

et al. 2023

View full text Add to dashboard Cite

The high prevalence of type 2 diabetes mellitus (T2DM), and the lack of effective therapy, determine the need for new treatment options. The present study is focused on the NO-donors drug class as effective antidiabetic agents. Since numerous biological systems are involved in the pathogenesis and progression of T2DM, the most promising approach to the development of effective drugs for the treatment of T2DM is the search for pharmacologically active compounds that are selective for a number of therapeutic targets for T2DM and its complications: oxidative stress, non-enzymatic protein glycation, polyol pathway. The nitrosyl iron complex with thiosulfate ligands was studied in this work. Binuclear iron nitrosyl complexes are synthetic analogues of [2Fe–2S] centers in the regulatory protein natural reservoirs of NO. Due to their ability to release NO without additional activation under physiological conditions, these compounds are of considerable interest for the development of potential drugs. The present study explores the effects of tetranitrosyl iron complex with thiosulfate ligands (TNIC-ThS) on T2DM and its complications regarding therapeutic targets in vitro, as well as its ability to bind liposomal membrane, inhibit lipid peroxidation (LPO), and non-enzymatic glycation of bovine serum albumin (BSA), as well as aldose reductase, the enzyme that catalyzes the reduction in glucose to sorbitol in the polyol pathway. Using the fluorescent probe method, it has been shown that TNIC-ThS molecules interact with both hydrophilic and hydrophobic regions of model membranes. TNIC-ThS inhibits lipid peroxidation, exhibiting antiradical activity due to releasing NO (IC50 = 21.5 ± 3.7 µM). TNIC-ThS was found to show non-competitive inhibition of aldose reductase with Ki value of 5.25 × 10−4 M. In addition, TNIC-ThS was shown to be an effective inhibitor of the process of non-enzymatic protein glycation in vitro (IC50 = 47.4 ± 7.6 µM). Thus, TNIC-ThS may be considered to contribute significantly to the treatment of T2DM and diabetic complications.

show abstract

Section: Resultsmentioning

confidence: 99%

Influence of Nitrosyl Iron Complex with Thiosulfate Ligands on Therapeutically Important Targets Related to Type 2 Diabetes Mellitus

et al. 2023

View full text Add to dashboard Cite

show abstract

“…NO formed as a result of HNO oxidation can also stop free radical lipid oxidation since it interacts with hydroperoxide radicals [ 53 , 54 , 55 , 56 ]. NO can effectively produce reactions with ROO • and RO • with the rate constant of k = 2 × 10 9 M −1 s −1 [ 54 ].…”

Section: Resultsmentioning

confidence: 99%

“…Under oxidative stress, HNO increases the viability of yeast cells deficient in coenzyme Q and inhibits LPO [ 19 ] that arises from reduction of free lipid radicals. Moreover, through HNO oxidation, NO is formed, which may also exhibit antioxidant properties and can stop LPO reactions [ 53 , 54 , 55 , 56 , 62 , 63 ]. HNO can reduce superoxide production both by inhibiting NADH oxidase [ 64 ] and by inhibiting mitochondrial respiratory chain complexes I and II [ 65 ].…”

Section: Discussionmentioning

confidence: 99%

Antiglycation and Antioxidant Effect of Nitroxyl towards Hemoglobin

et al. 2022

View full text Add to dashboard Cite

Donors of nitroxyl and nitroxyl anion (HNO/NO−) are considered to be promising pharmacological treatments with a wide range of applications. Remarkable chemical properties allow nitroxyl to function as a classic antioxidant. We assume that HNO/NO− can level down the non-enzymatic glycation of biomolecules. Since erythrocyte hemoglobin (Hb) is highly susceptible to non-enzymatic glycation, we studied the effect of a nitroxyl donor, Angeli’s salt, on Hb modification with methylglyoxal (MG) and organic peroxide―tert-butyl hydroperoxide (t-BOOH). Nitroxyl dose-dependently decreased the amount of protein carbonyls and advanced glycation end products (AGEs) that were formed in the case of Hb incubation with MG. Likewise, nitroxyl effectively protected Hb against oxidative modification with t-BOOH. It slowed down the destruction of heme, formation of carbonyl derivatives and inter-subunit cross-linking. The protective effect of nitroxyl on Hb in this system is primarily associated with nitrosylation of oxidized Hb and reduction of its ferryl form, which lowers the yield of free radical products. We suppose that the dual (antioxidant and antiglycation) effect of nitroxyl makes its application possible as part of an additional treatment strategy for oxidative and carbonyl stress-associated diseases.

show abstract

“…Similar spectra were observed earlier at 77 K and room temperature for the albumin-bound NICs. 22,65,66 The concentration of paramag-netic centers is 0.76 mM; after a day, their concentration does not change. The observed anisotropy of the g-factor indicates that the rotation of paramagnetic centers is strongly inhibited due to their binding to the albumin molecule.…”

Section: Dalton Transactions Papermentioning

confidence: 99%

A nitrosyl iron complex with 3.4-dichlorothiophenolyl ligands: synthesis, structures and its reactions with targets – carriers of nitrogen oxide (NO) in vivo

et al. 2023

View full text Add to dashboard Cite

show abstract

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

Cited by 9 publications

References 44 publications

Influence of Nitrosyl Iron Complex with Thiosulfate Ligands on Therapeutically Important Targets Related to Type 2 Diabetes Mellitus

Influence of Nitrosyl Iron Complex with Thiosulfate Ligands on Therapeutically Important Targets Related to Type 2 Diabetes Mellitus

Antiglycation and Antioxidant Effect of Nitroxyl towards Hemoglobin

A nitrosyl iron complex with 3.4-dichlorothiophenolyl ligands: synthesis, structures and its reactions with targets – carriers of nitrogen oxide (NO) in vivo

Contact Info

Product

Resources

About