Binuclear nitrosyl iron complex with 4-acetamidothiophenolyl: Synthesis and study of its decomposition in a system with glutathione and albumin

• Published in: Polyhedron Vol. 250; p. 116819
• Main Authors: Pokidova, Olesya V., Novikova, Veronika O., Emel'yanova, Nina S., Mazina, Ludmila M., Konyukhova, Alina S., Ovanesyan, Nikolai S., Kulikov, Alexander V., Balakina, Anastasiya A., Sanina, Natalia A.
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01-03-2024
• Subjects: Albumin; Glutathione; Griess test; Nitrosyl iron complexes; Quantum-chemical calculations; Albumin; Nitrosyl iron complexes; Griess test; Glutathione; Quantum-chemical calculations
• ISSN: 0277-5387
• DOI: 10.1016/j.poly.2023.116819

A new binuclear nitrosyl iron complex with 4-acetamidothiophenolyl is synthesized. In DMSO, the complex decomposes into mononuclear fragments; in water, it is binuclear and rapidly releases NO. In albumin, the complex does not form high molecular weight products and generates NO slowly. Glutathione does not affect the decay of complex.
[Display omitted]
In this work, we synthesized a new binuclear nitrosyl iron complex of the family of Roussin's red salt ester [Fe2(C8H8NOS)2(NO)4] (complex 1) with 4-acetamidothiophenol (a structural analog of acetaminophen), which generates NO during hydrolysis and is promising for treatment socially significant diseases. It has been established that solvents have a significant effect on the process of its decomposition: in a buffer solution, complex 1 retains its binuclear structure, while in DMSO it forms mononuclear iron-nitrosyl products. Reduced glutathione does not replace 4-acetamidothiophenol ligands in the structure of complex 1. In addition, complex 1 and its products are not coordinated with the known binding sites of bovine serum albumin, including Cys34. It was found that the studied complex 1 is adsorbed on the protein surface due to weak intermolecular interactions, which leads to a decrease in the rate of decomposition, and, as a result, to a longer generation of NO.
Thus, it has been shown for the first time that compound 1 and its decay products do not form coordination complexes with the biosubstrates studied in this work. It can be assumed that glutathione will not participate in the transformation of complex 1 in vivo, while albumin, due to the effective stabilization of the complex on the surface, can act as its carrier to therapeutic targets.