Spectroscopic and molecular docking investigation on the interaction of a water-soluble Cu(II) complex containing diethanolamine and dipicolinic acid ligands with human serum albumin.
| Autor: | Shahabadi N; Department of Inorganic Chemistry, Faculty of Chemistry, Razi University, Kermanshah, Iran., Marzbani A; Department of Inorganic Chemistry, Faculty of Chemistry, Razi University, Kermanshah, Iran., Hadidi S; Department of Inorganic Chemistry, Faculty of Chemistry, Razi University, Kermanshah, Iran., Mardani Z; Inorganic Chemistry Department, Faculty of Chemistry, Urmia University, Urmia, Iran. |
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| Jazyk: | angličtina |
| Zdroj: | Journal of biomolecular structure & dynamics [J Biomol Struct Dyn] 2023 Dec 26, pp. 1-9. Date of Electronic Publication: 2023 Dec 26. |
| DOI: | 10.1080/07391102.2023.2297812 |
| Abstrakt: | Under physiological conditions, spectroscopic techniques as well as molecular docking simulation have been used to investigate the binding interaction mechanism between Cu(II) complex containing Pyridine-2,6-dicarboxylic acid (PDCA) and Diethanolamine (DEA) ligands, [Cu(DEA)(PDCA)] and human serum albumin (HSA). UV spectral changes of protein in the presence of the Cu(II) complex suggested the formation of a Protein-Cu(II) complex conjugate with specific new structure. The Cu(II) complex quenches the intrinsic fluorescence of the HSA via a static mechanism in which van der Waals interactions along with hydrogen bonds are fundamental binding forces. Displacement experiments performed by warfarin and ibuprofen site probes predict that the Cu(II) complex is located in subdomain IIA, Sudlow site 1 of HSA. Molecular docking results showed close resemblance with experimental data.Communicated by Ramaswamy H. Sarma. |
| Databáze: | MEDLINE |
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