Affinity to bovine serum albumin and anticancer activity of some new water-soluble metal Schiff base complexes

• Published in: Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy Vol. 133; pp. 697 - 706
• Main Authors: Asadi, Mozaffar, Asadi, Zahra, Zarei, Leila, Sadi, Somaye Barzegar, Amirghofran, Zahra
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 10.12.2014
• Subjects: Animals; Anticancer activity; Antineoplastic Agents - chemistry; Antineoplastic Agents - metabolism; Antineoplastic Agents - pharmacology; Benzylamines - chemistry; Benzylamines - metabolism; Benzylamines - pharmacology; Bovine serum albumin; Cattle; Cell Line, Tumor; Coordination Complexes - chemistry; Coordination Complexes - metabolism; Coordination Complexes - pharmacology; Fluorescence quenching; Humans; Neoplasms - drug therapy; Protein Binding; Schiff base; Schiff Bases - chemistry; Schiff Bases - metabolism; Schiff Bases - pharmacology; Serum Albumin, Bovine - chemistry; Serum Albumin, Bovine - metabolism; Solubility; Thermodynamics; Water - chemistry; Schiff base; Bovine serum albumin; Anticancer activity; Fluorescence quenching
• ISSN: 1386-1425; 1873-3557
• DOI: 10.1016/j.saa.2014.05.031

Effect of water soluble Schiff base complex, on the fluorescence spectra of BSA has been investigated. [Display omitted] •Synthesis and characterization of new water-soluble Schiff base complexes Na2 [M(5-SO3-1,2-salben)] are studied.•The formation constants, Kf, of the complexes are calculated spectroscopically.•Affinity of [M(5-SO3-1,2-salben)]2− to bovine serum albumin are studied by fluorimetry method.•The growth inhibitory of the complexes is studied. Metal Schiff-base complexes show biological activity but they are usually insoluble in water so four new water-soluble metal Schiff base complexes of Na2[M(5-SO3-1,2-salben]; (5-SO3-1,2-salben denoted N,N′-bis(5-sulphosalicyliden)-1,2-diaminobenzylamine and M=Mg, Mn, Cu, Zn) were synthesized and characterized. The formation constants of the metal complexes were determined by UV–Vis absorption spectroscopy. The interaction of these complexes with bovine serum albumin (BSA) was studied by fluorescence spectroscopy. Type of quenching, binding constants, number of binding sites and binding stoichiometries were determined by fluorescence quenching method. The results showed that the mentioned complexes strongly bound to BSA. Thermodynamic parameters indicated that hydrophobic association was the major binding force and that the interaction was entropy driven and enthalpically disfavoured. The displacement experiment showed that these complexes could bind to the subdomain IIA (site I) of albumin. Furthermore the synchronous fluorescence spectra showed that the microenvironment of the tryptophan residues was not apparently changed. Based on the Förster theory of non-radiation energy transfer, the distance between the donor (Trp residues) and the acceptor metal complexes was obtained. The growth inhibitory effect of complexes toward the K562 cancer cell line was measured.