albumin - publications
Synthesis, characterization and interaction studies of copper based drug with Human Serum Albumin (HSA): Spectroscopic and molecular docking investigations.
J Photochem Photobiol B. 2012 Jun 15;
Authors: Tabassum S, Al-Asbahy WM, Afzal M, Arjmand F
A new water soluble copper(II) complex, [Cu(glygly)(ssz)(H(2)O)]Ã¢ÂÂ 6H(2)O, 1 derived from dipeptide (glycyl glycine anion) and sulfasalazine was synthesized and characterized by elemental analysis (CHN), molar conductance measurements and spectroscopic methods (IR, UV-vis, ESI-MS). The complex 1 is non-ionic in nature and possess octahedral geometry around Cu(II) metal ion. The interaction of complex 1 with Human Serum Albumin (HSA) was investigated under physiological condition in Tris-HCl buffer solution at pH 7.4 by means of various spectroscopic methods (fluorescence, CD and FTIR) and molecular docking technique. The results of fluorescence titration revealed that the complex 1 strongly quench the intrinsic fluorescence of HSA through a static quenching procedure. Binding constants (K(b)) and the number of binding sites (nÃ¢ÂÂ1) were calculated using modified Stern-Volmer equations. The thermodynamic parameters ÃÂG at different temperatures were calculated subsequently the value of ÃÂH and ÃÂS was also calculated which revealed that the hydrophobic and hydrogen bonding interactions play a major role in HSA-complex 1 association. The distance r between donor (HSA) and acceptor (complex 1) was obtained according to fluorescence resonance energy transfer and the alterations of HSA secondary structure induced by complex 1 were confirmed by FT-IR and CD measurements.
PMID: 22750083 [PubMed - as supplied by publisher]