INFIQC   05475
INSTITUTO DE INVESTIGACIONES EN FISICO- QUIMICA DE CORDOBA
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Study of the association between a serum albumine and a new cobalt complex
Autor/es:
P. F. GARCIA; C. CORONEL; A. VELO; A. SINGH; R. P. SHARMA; G. A. ARGüELLO
Lugar:
Buenos Aires
Reunión:
Congreso; XL Reunión Anual de la Sociedad Argentina de Biofisica; 2011
Institución organizadora:
Sociedad argentina de Biofísica
Resumen:
The Photodynamic Therapy (PDT) has emerged as an attractive option for the treatment of cancer pathologies1, thanks to the study and utilization of transition metal complexes (among other) as photosensitizers.2  Bovine Seric Albumine (BSA) is a well studied protein due to its ability to act as carrier for number of substrates to the interior of cell. The aim of this work was to study the binding between Bovine Seric Albumine (BSA) and a new cationic cobalt(III) complex, [Co(phen)(H2biim)2]3+ synthesized by Dr. R. P. Sharma et al.      The fluorescence quenching of the protein by the cationic cobalt(III) complex at different excitation wavelength and at different temperatures has been studied. It was observed that both tryptophan as well as tyrosine residues are involved in the quenching processes, as also observed in our earlier studies3 .  Using the Bhattacharya`s model, association constant (Kb) were determined which render a value around 9x104 at room temperature.  By the study of Kb at different temperatures and using the Van`t Hoff equation it was possible to evaluated the thermodynamics parameters. ÄH=6,65kJ/mol, ÄS=117,3J/mol.K and ÄG= -28,3kJ/mol      In conclusion, the complex and the protein bind spontaneously and the association is an endothermic process. According to the thermodynamic parameters, the acting forces are mainly hydrophobic interactions, although the electrostatic attraction cannot be discarded.3