Interaction of water-soluble amino acid Schiff base complexes with bovine serum albumin: fluorescence and circular dichroism studies.
Fluorescence spectroscopy in combination with circular dichroism (CD) spectroscopy were used to investigate the interaction of water-soluble amino acid Schiff base complexes, [Zn(L1,2)(phen)] where phen is 1,10-phenanthroline and H2L1,2 is amino acid Schiff base ligands, with bovine serum albumin (BSA) under the physiological conditions in phosphate buffer solution adjusted to pH 7.0. The quenching mechanism of fluorescence was suggested as static quenching according to the Stern-Volmer equation. Quenching constants were determined using the Stern-Volmer equation to provide a measure of the binding affinity between amino acid Schiff base complexes and BSA. The thermodynamic parameters DeltaG, DeltaH and DeltaS at different temperatures (298, 310 and 318K) were calculated. The results indicate that the hydrophobic and hydrogen bonding interactions play a major role in [Zn(L1)(phen)]-BSA association, whereas hydrophobic and electrostatic interactions participate a main role in [Zn(L2)(phen)]-BSA binding process. Binding studies concerning the number of binding sites and apparent binding constant Kb were performed by fluorescence quenching method. The distance R between the donor (BSA) and acceptor (amino acid Schiff base complexes) has been obtained utilizing fluorescence resonant energy transfer (FRET). Furthermore, CD spectra were used to investigate the structural changes of the BSA molecule with the addition of amino acid Schiff base complexes. The results indicate that the interaction of amino acid Schiff base complexes with BSA leads to changes in the secondary structure of the protein. Fractional contents of the secondary structure of BSA (f(alpha), f(beta), f(turn) and f(random)) were calculated with and without amino acid Schiff base complexes utilizing circular dichroism spectroscopy. Our results clarified that amino acid Schiff base complexes could bind to BSA and be effectively transported and eliminated in the body, which could be a useful guideline for further drug design.
Gharagozlou
Mehrnaz
M
Department of Nanotechnology and Nanomaterials, Institute for Colorants, Paint and Coatings, P.O. Box 16765-654, Tehran, Iran.
Boghaei
Davar M
DM
D000818:Animals; D002417:Cattle; D002626:Chemistry, Pharmaceutical / Q000379:methods; D002942:Circular Dichroism / Q000379:methods*; D015195:Drug Design; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods; D007700:Kinetics; D011485:Protein Binding; D017433:Protein Structure, Secondary; D012545:Schiff Bases / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D012995:Solubility; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013816:Thermodynamics; D014867:Water / Q000737:chemistry*
D012545:Schiff Bases; D014867:Water; D012710:Serum Albumin, Bovine