Adducts of bovine serum albumin and binuclear nitrosyl iron complex with thiosulfate ligands: a molecular docking and quantum chemical study

被引：1

作者：

Emel'yanova, N. S. ^{[1
]}

Zhilenkov, A. V. ^{[1
]}

Pokidova, O. V. ^{[1
]}

Gutsev, L. G. ^{[1
]}

Zagainova, E. A. ^{[1
]}

Sanina, N. A. ^{[1
]}

Aldoshin, S. M. ^{[1
]}

机构：

[1] Russian Acad Sci, Fed Res Ctr Problems Chem Phys & Med Chem, Prosp Akad Semenova 1, Moscow 142432, Russia

来源：

RUSSIAN CHEMICAL BULLETIN | 2024年 / 73卷 / 09期

关键词：

nitrosyl complexes; albumin; molecular docking; time-dependent density functional theory (TDDFT); QTAIM; NITRIC-OXIDE; HEMOGLOBIN; THIOUREA;

D O I：

10.1007/s11172-024-4369-5

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A molecular docking study aimed at shedding light on the binding mechanisms of a nitrosyl iron complex to bovine serum albumin (BSA) revealed three possible binding sites. Main types of bonds were established. The complex-BSA binding energies at different sites were determined using the AutoDockTools program and from QTAIM analysis. Docking with inclusion of water molecules led to shielding of one binding site (only two binding sites remain) and to a better agreement between the binding energies obtained by two different methods. Electronic spectra of the resulting molecular complexes were simulated in terms of the time-dependent density functional theory (TDDFT). The changes in the experimental spectrum as well as stabilization of the nitrosyl iron complexes by BSA were explained.

引用

页码：2583 / 2592

页数：10

共 40 条

[1] Formation of supramolecular synthons in the crystalline structure of the dinitrosyl iron complexes with aliphatic thiourea ligands [J].