Features of interaction of tetraiodide meso-tetra(N-methyl-3-pyridyl)porphyrin with bovine serum albumin

• Published in: Journal of molecular liquids 2018-09, Vol.265, p.664-667
• Main Authors: Lebedeva, Natalia Sh, Gubarev, Yury A., Yurina, Elena S., Syrbu, Sergey A.
• Format: Article
• Language: English
• Subjects: 5,10,15,20-Tetrakis(1-methyl-4-pyridinio)porphyrin; Albumin; Fluorescence quenching; Fluoresces; Porphyrins; Scatchard constants
• ISSN: 0167-7322; 1873-3166
• DOI: 10.1016/j.molliq.2018.06.030

The interaction processes spectral study of tetraiodide meso-tetra(N-methyl-3-pyridyl)porphyrin with blood serum albumin has been carried out. The results obtained are considered in comparison with similar data for tetraphenylporphyrin and tetraiodide meso-tetra(N-methyl-4-pyridyl)porphyrin. It is established that interaction of albumin with the porphyrins under study leads to a change in the secondary structure of the protein accompanied by a decrease in the proportion of disordered fragments of the protein and an increase in β-structuring within the complexes. NCH3+ group isomerism position in the porphyrin compound significantly affects binding to albumin. Adding of the substituent in meta-position of the phenyl ring contributes to the increased affinity of protein to the cationic porphyrin, compared to the pair-substituted counterpart. •Binding characteristics of porphyrins with protein were studied.•The binding constants and binding distance were calculated by using Scatchard method.•Localization of porphyrin on the protein globule is defined.