EUROPEAN JOURNAL OF
PHARMACEUTICAL AND MEDICAL RESEARCH

( An ISO 9001:2015 Certified International Journal )

An International Peer Reviewed Journal for Pharmaceutical, Medical & Biological Sciences

An Official Publication of Society for Advance Healthcare Research (Reg. No. : 01/01/01/31674/16)

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 ISSN 2394-3211

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Abstract

PROTEIN BINDING OF CHLORTHALIDONE AND ITS INTERACTION WITH FOOD

*Gayathri V., Jeeshna G., Nandhini S. and Sangavi M. S.

ABSTRACT

Chlorthalidone is a thiazide-like diuretic that leads to fluid retention and was approved for the treatment of hypertension either individually or in combination with other Hypertension drugs. Chlorthalidone is poorly soluble in water at room temperature and soluble in Ethanol, Methanol and Sodium hydroxide. The objective of this study is to estimate the protein binding of chlorthalidone individually and in presence of grape juice. UV spectral studies authenticate the spectra obtained were matched with standard pure drug UV spectra show the maximum absorbance peak at 260 nm. The concentration of Chlorthalidone having affinity towards Protein across the Semipermeable membrane is determined. Interactions between food and drugs can unintentionally reduce or increase the effect of the drug, resulting in alteration of desired therapeutic activity. Food drug interaction is conducted for this drug using Grape juice as a food content and the concentration of the bound and unbound drug is determined using UV spectral absorbance of the drug. Hence based on the observation performed at invitro, protein binding studies of chlorthalidone individually and in combination with grape juice, it was observed that the concentration of unbound drug was found to increase in presence of grape juice at various time intervals as compared to the drug individually administered. Hence it can be concluded that there was a significant interaction between chlorthalidone and grape juice at invitro level which has to further conformed by pursuing the invivo study.

Keywords: chlorthalidone, interaction, protein binding.


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