Binding of an anti-inflammatory drug lornoxicam with blood proteins

Insights from spectroscopic investigations

Reeta Punith, Ashwini H. Hegde, Seetharamappa Jaldappagari

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

The interaction between an anti-inflammatory drug, lornoxicam (LXM) and protein (human serum albumin and bovine serum albumin) was studied by spectroscopic techniques (Fluorescence, synchronous, FT-IR, UV-vis absorption and circular dichroism). The quenching mechanism of fluorescence of the protein by the drug was discussed. Based on the interaction studies carried out at different temperatures by spectrofluorometry, the binding constant and the number of binding sites for drug on protein have been evaluated. The nature of binding force operating between the drug and protein was proposed to be electrostatic and hydrophobic based on thermodynamic parameters. The distance r between the donor (protein) and acceptor (drug) was determined based on the Förster's theory of nonradiation energy transfer and found to be 2.38 nm and 2.56 nm for LXM-BSA and LXM-HSA respectively. Displacement studies with different site probes revealed that the drug bound to the hydrophobic pocket located in sub domain IIA; that is to say, Trp-214 was near or within the binding site. Circular dichroism data of protein in the presence of drug revealed the decreased a-helicity and hence changes in secondary structure of protein. The effects of some common ions were also investigated.

Original languageEnglish
Pages (from-to)487-495
Number of pages9
JournalJournal of Fluorescence
Volume21
Issue number2
DOIs
Publication statusPublished - 01-03-2011

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Blood Proteins
Anti-Inflammatory Agents
drug
Pharmaceutical Preparations
Proteins
Circular Dichroism
Fluorescence
Binding Sites
Secondary Protein Structure
Fluorescence Spectrometry
Energy Transfer
Bovine Serum Albumin
interaction
lornoxicam
Static Electricity
Thermodynamics
Serum Albumin
Energy transfer
Electrostatics
Quenching

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Clinical Psychology
  • Social Sciences (miscellaneous)
  • Sociology and Political Science
  • Spectroscopy
  • Clinical Biochemistry
  • Law

Cite this

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abstract = "The interaction between an anti-inflammatory drug, lornoxicam (LXM) and protein (human serum albumin and bovine serum albumin) was studied by spectroscopic techniques (Fluorescence, synchronous, FT-IR, UV-vis absorption and circular dichroism). The quenching mechanism of fluorescence of the protein by the drug was discussed. Based on the interaction studies carried out at different temperatures by spectrofluorometry, the binding constant and the number of binding sites for drug on protein have been evaluated. The nature of binding force operating between the drug and protein was proposed to be electrostatic and hydrophobic based on thermodynamic parameters. The distance r between the donor (protein) and acceptor (drug) was determined based on the F{\"o}rster's theory of nonradiation energy transfer and found to be 2.38 nm and 2.56 nm for LXM-BSA and LXM-HSA respectively. Displacement studies with different site probes revealed that the drug bound to the hydrophobic pocket located in sub domain IIA; that is to say, Trp-214 was near or within the binding site. Circular dichroism data of protein in the presence of drug revealed the decreased a-helicity and hence changes in secondary structure of protein. The effects of some common ions were also investigated.",
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Binding of an anti-inflammatory drug lornoxicam with blood proteins : Insights from spectroscopic investigations. / Punith, Reeta; Hegde, Ashwini H.; Jaldappagari, Seetharamappa.

In: Journal of Fluorescence, Vol. 21, No. 2, 01.03.2011, p. 487-495.

Research output: Contribution to journalArticle

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