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Original Research Article | OPEN ACCESS

Binding Studies of Lamotrigine with Sera of Different Animal Species

Kalyan Kumar Sen1 , Sanat Kumar Basu2, Sadhan Kumar Dutta1

1Pharmacy Divisions, Gupta College of Technological Sciences, Ashram More, G.T. Road, Asansol-713301; 2Department of Pharmaceutical Technology, Jadavpur University, Kolkata-700032, India.

For correspondence:-  Kalyan Sen   Email: kkskpa@gmail.com   Tel:+919932334958

Received: 25 October 2008        Accepted: 17 July 2009        Published: 23 October 2009

Citation: Sen KK, Basu SK, Dutta SK. Binding Studies of Lamotrigine with Sera of Different Animal Species. Trop J Pharm Res 2009; 8(5):409-415 doi: 10.4314/tjpr.v8i5.5

© 2009 The authors.
This is an Open Access article that uses a funding model which does not charge readers or their institutions for access and distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0) and the Budapest Open Access Initiative (http://www.budapestopenaccessinitiative.org/read), which permit unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited..

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 methanol-water solvent (1:1 and 1:3) with horse serum at 20, 28 and 37 0C  The equilibrium dialysis evaluation of lamotrigine with sera of other animal species - rabbit, goat and rat - was also performed at 37 0C.
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 DHvalue and a small positive DS 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

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Thompson Reuters (ISI): 0.523 (2021)
H-5 index (Google Scholar): 39 (2021)

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