Binding mechanism of bioactive cetirizine hydrochloride to sudlow's site i of serum albumins

Ashwini H. Hegde, B. Sandhya, Shankara S. Kalanur, J. Seetharamappa

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

The mechanism of interaction of an anti-allergic drug, cetirizine dihydrochloride, with the proteins bovine and human serum albumins has been investigated by spectrofluorimetry, FTIR, UV-vis absorption and circular dichroism methods at physiological conditions. The drug was found to quench the fluorescence intensity of the protein through a dynamic quenching mechanism. Various binding parameters were evaluated based on fluorescence quenching studies carried out at 293 K, 301 K and 308 K. The nature of the binding force operating between the drug and protein was proposed, based on the measured thermodynamic parameters. A change in the secondary structure of the protein was evident from the circular dichroism measurements, wherein the α-helicity decreased from 65.69% to 51.23% and from 42.7% to 38.55% for the CTZ-BSA and CTZ-HSA systems, respectively. Based on Förster's theory of non-radiative energy transfer, the distance between the protein and drug was determined. The common blood plasma ions K+, Cu2+, Ni2+, Mn2+ and Co2+ were found to influence the binding of the drug to the protein. Displacement experiments were carried out to determine the binding site for drug on the protein. These studies, coupled with other spectroscopic results, revealed that the drug was bound to the hydrophobic pocket located in sub domain IIA of site I.

Original languageEnglish
Pages (from-to)182-197
Number of pages16
JournalJournal of Solution Chemistry
Volume40
Issue number2
DOIs
Publication statusPublished - 01-02-2011

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Cetirizine
hydrochlorides
activity (biology)
albumins
Serum Albumin
serums
drugs
proteins
Pharmaceutical Preparations
Proteins
Circular Dichroism
dichroism
Quenching
Fluorescence
quenching
Secondary Protein Structure
blood plasma
Anti-Allergic Agents
fluorescence
Energy Transfer

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Physical and Theoretical Chemistry

Cite this

Hegde, Ashwini H. ; Sandhya, B. ; Kalanur, Shankara S. ; Seetharamappa, J. / Binding mechanism of bioactive cetirizine hydrochloride to sudlow's site i of serum albumins. In: Journal of Solution Chemistry. 2011 ; Vol. 40, No. 2. pp. 182-197.
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Binding mechanism of bioactive cetirizine hydrochloride to sudlow's site i of serum albumins. / Hegde, Ashwini H.; Sandhya, B.; Kalanur, Shankara S.; Seetharamappa, J.

In: Journal of Solution Chemistry, Vol. 40, No. 2, 01.02.2011, p. 182-197.

Research output: Contribution to journalArticle

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