ARGÜELLO GERARDO ANÍBAL
Congresos y reuniones científicas
Título:
Study of the association between a serum albumine and a new cobalt complex
Autor/es:
PABLO F. GARCÍA; CONSUELO CORONEL; ALEJANDRA VELO; AJNESH SINGH; RAJ PAL SHARMA; ARGÜELLO, GERARDO ANÍBAL
Lugar:
Bs. As.
Reunión:
Congreso; SAB-Reunión Annual de la Sociedad Argentina de Biofísica; 2011
Resumen:

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.