title: Affinity to bovine serum albumin and anticancer activity of some new water-soluble metal Schiff base complexes.
abstract: 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.
authors.affiliation: Chemistry Department, College of Sciences, Shiraz University, Shiraz 71454, Islamic Republic of Iran. Electronic address: asadi@susc.ac.ir.
authors.forename: Mozaffar
authors.initials: M
authors.lastname: Asadi
authors.affiliation: Chemistry Department, College of Sciences, Shiraz University, Shiraz 71454, Islamic Republic of Iran.
authors.forename: Zahra
authors.initials: Z
authors.lastname: Asadi
authors.affiliation: Chemistry Department, College of Sciences, Shiraz University, Shiraz 71454, Islamic Republic of Iran.
authors.forename: Leila
authors.initials: L
authors.lastname: Zarei
authors.affiliation: Chemistry Department, College of Sciences, Shiraz University, Shiraz 71454, Islamic Republic of Iran.
authors.forename: Somaye Barzegar
authors.initials: SB
authors.lastname: Sadi
authors.affiliation: Immunology Department, Shiraz University of Medical Sciences, Shiraz 71454, Islamic Republic of Iran.
authors.forename: Zahra
authors.initials: Z
authors.lastname: Amirghofran
mesh_terms: D000818:Animals; D000970:Antineoplastic Agents / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D001596:Benzylamines / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D002417:Cattle; D045744:Cell Line, Tumor; D056831:Coordination Complexes / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D006801:Humans; D009369:Neoplasms / Q000188:drug therapy; D011485:Protein Binding; D012545:Schiff Bases / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D012995:Solubility; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
chemical_list: D000970:Antineoplastic Agents; D001596:Benzylamines; D056831:Coordination Complexes; D012545:Schiff Bases; D014867:Water; D012710:Serum Albumin, Bovine
keywords: Anticancer activity; Bovine serum albumin; Fluorescence quenching; Schiff base