| Info. | Vol.10 - No.1 (2016.03.20) |
|---|---|
| Title | Spectral and Hydrodynamic Studies of Complex Formation of Tetraalkoxy Substituted Zinc(II)phthalocyanines with Defatted and Nondefatted Bovine Serum Albumin |
| Authors | Natalya Lebedeva1, Elena Malkova1, Anatoly Vyugin1, Oscar Koifman2 & Yury Gubarev1,* |
| Institutions | 1G.A. Krestov Institute of Solution Chemistry of the Russian academy
of Sciences, Russia 2Research Institute of Macroheterocycles, Ivanovo State University of Chemical Technology, Russia |
| Abstract | Spectral, hydrodynamic and thermochemical studies have been demonstrated that tetraalkoxy substituted zinc(II)phthalocyanines form stable complexes with defatted and nondefatted bovine serum albumin. The phthalocyanines interact with BSA through heteroatoms of their peripheral substitutes. It was found that ZnPc(4-NH-CO-C6H4-OC3H7)4 is located in the protein subdomains IB and IIA whereas ZnPc(4-NHCO- C6H4-OC6H13)4 and ZnPc(4-NH-CO-C6H4-OC8H17)4 are immobilized on surface of the protein globule at a distance of not greater than 10 nm from the tryptophan residues in the positions 135 and 214 of the protein polypeptide chain. Zinc(II)phthalocyanines (ZnPc(4-NH-CO-C6H4-OC6H13)4 and ZnPc(4-NH-CO-C6H4-OC8H17)4) increase thermal stability of BSA. |
| Keyword | Phthalocyanine, Albumin, Fatty acid, Complexes, Spectroscopy |
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