![](/imgs/covers/pr_cover.jpg)
|
Tropical Journal of Pharmaceutical Research
Pharmacotherapy Group, Faculty of Pharmacy, University of Benin, Benin City, Nigeria
ISSN: 1596-5996 EISSN: 1596-5996
Vol. 8, No. 5, 2009, pp. 409-415
|
Bioline Code: pr09053
Full paper language: English
Document type: Research Article
Document available free of charge
|
|
Tropical Journal of Pharmaceutical Research, Vol. 8, No. 5, 2009, pp. 409-415
en |
Binding Studies of Lamotrigine with Sera of Different Animal Species
Sen, Kalyan Kumar; Basu, Sanat Kumar & Dutta, Sadhan Kumar
Abstract
Purpose:
The serum protein-binding characteristic of lamotrigine with sera from various species (horse,
rat, rabbit and goat) was studied at different dielectric constants and temperatures to obtain an insight
into the mechanism of interaction, evaluate the effect of dielectric constant on binding affinity, and to
determine the effect of species variation on drug plasma-protein interaction.
Method:
Binding data were generated by evaluating equilibrium dialysis of lamotrigine in methanolwater
solvent (1:1 and 1:3) with horse serum at 20, 28 and 37°C The equilibrium dialysis evaluation of
lamotrigine with sera of other animal species - rabbit, goat and rat - was also performed at 37°C.
Results:
A Rosenthal plot obtained with the binding data at different temperatures showed that binding
constant decreased with increasing temperature and that binding of lamotrigine to horse serum
appeared to be saturation binding. The results also indicated that the binding process was characterized
by negative DH0 value and a small positive ΔS0 values. The binding constant decreased as dielectric
constant rose.
Conclusions:
The results obtained suggest that hydrophobic interaction may have occurred and that
van der Waals’ forces were responsible for binding in the hydrophobic region. Data obtained for
lamotrigine binding with horse, goat, rabbit and rat sera show that there are no significant changes in
plasma protein binding in the above-mentioned species.
Keywords
Lamotrigine; Serum protein binding; Dielectric constant; Binding constant; Animal sera
|
|
© Copyright © Pharmacotherapy Group, Faculty of Pharmacy, University of Benin, Benin City, 300001 Nigeria. Alternative site location: http://www.tjpr.org
|
|