Study of the association between a serum albumine and a new cobalt complex

PABLO F. GARCÍA; CONSUELO CORONEL; ALEJANDRA VELO; AJNESH SINGH; RAJ PAL SHARMA; ARGÜELLO, GERARDO ANÍBAL

Bs. As.

Congreso; SAB-Reunión Annual de la Sociedad Argentina de Biofísica; 2011

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.1 , 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.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.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.2biim)2]3+ synthesized by Dr. R. P. Sharma et al.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. YH=6,65kJ/mol, YS=117,3J/mol.K and YG= -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 . 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. YH=6,65kJ/mol, YS=117,3J/mol.K and YG= -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.4 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. YH=6,65kJ/mol, YS=117,3J/mol.K and YG= -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.Kb at different temperatures and using the Van`t Hoff equation it was possible to evaluated the thermodynamics parameters. YH=6,65kJ/mol, YS=117,3J/mol.K and YG= -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.H=6,65kJ/mol, YS=117,3J/mol.K and YG= -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.