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Indian Journal of Experimental Biology (IJEB) >
IJEB Vol.44 [2006] >
IJEB Vol.44(02) [February 2006] >
| Title: | Binding of diclofenac sodium with bovine serum albumin at different temperatures, pH and ionic strengths |
| Authors: | Dutta, S K
Basu, S K
Sen, K K |
| Keywords: | Albumin
Bovine serum
Diclofenac sodium
Ionic strength |
| Issue Date: | Feb-2006 |
| Publisher: | CSIR |
| Abstract: | The study was designed to examine the binding of
diclofenac sodium with bovine serum albumin (BSA) at different temperatures (20°, 30° and 40°C), pH (6.4,7.4
and 8.4) and ionic strengths ( = 0.1,
0.2 and 0.3) by means of equilibrium dialysis method. The concentration of
diclofenac sodium was maintained at wider range from 15 to 900 mole/l and BSA concentration was maintained at 61.5 mole/l. The data obtained were interpreted by nonlinear regression
method using Graphpad prism software. The analysis showed that the interaction
between diclofenac sodium with BSA results in two-site saturable binding. A
decrease in association constant was observed with increasing temperature. The
average standard free energy change (ΔG°) value was –7.07 (site I) and –4.2 (site II) Kcal/mol. The standard
enthalpy change (ΔH°) and the standard entropy change (ΔS°) were–7.8 Kcal/mole, –2.35 cal/mole
(site I) and –7.4 Kcal/mole, –10.5 cal/mole (site II), respectively. The
negative enthalpy change suggested the binding between diclofenac sodium and
the binding sites of BSA were spontaneous and exothermic. The negative value of
ΔH° and ΔS° indicated hydrogen bonding and van der
Waal’s force was the major mechanism for diclofenac sodium and BSA interaction.
Increase in pH and ionic strength
also caused decrease in association constant of diclofenac sodium and BSA
binding. |
| Page(s): | 123-127 |
| ISSN: | 0975-1009 (Online); 0019-5189 (Print) |
| Source: | IJEB Vol.44(02) [February 2006]
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