Exploring the binding mechanism of ondansetron hydrochloride to serum albumins: Spectroscopic approach

B. Sandhya, Ashwini H. Hegde, K. C. Ramesh, J. Seetharamappa

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

The mechanism of interaction of ondansetron hydrochloride (OND) to serum albumins [bovine serum albumin (BSA) and human serum albumin (HSA)] was studied for the first time employing fluorimetric, circular dichroism, FTIR and UV-vis absorption techniques under the simulated physiological conditions. Fluorimetric results were utilized to investigate the binding and conformational characteristics of protein upon interaction with varying concentrations of the drug. Higher binding constant values revealed the strong interaction between the drug and protein while the number of binding sites close to unity indicated single class of binding site for OND in protein. Thermodynamic results revealed that both hydrogen bond and hydrophobic interactions played a major role in stabilizing drug-protein complex. Site marker competitive experiments indicated that the OND bound to albumins at subdomin II A (Sudlow's site I). Further, the binding distance between OND and serum albumin was calculated based on the Förster's theory of non-radioactive energy transfer and found to be 2.30 and 3.41 nm, respectively for OND-BSA and OND-HSA. The circular dichroism data revealed that the presence of OND decreased the α-helix content of serum albumins. 3D-fluorescence results also indicated the conformational changes in protein upon interaction with OND. Further, the effects of some cations have been investigated in the interaction of drug to protein.

Original languageEnglish
Pages (from-to)410-416
Number of pages7
JournalSpectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
Volume86
DOIs
Publication statusPublished - 01-02-2012

Fingerprint

Ondansetron
hydrochlorides
albumins
Serum Albumin
serums
Proteins
proteins
drugs
Dichroism
Binding sites
Bovine Serum Albumin
Pharmaceutical Preparations
dichroism
interactions
Binding Sites
Energy transfer
Hydrogen bonds
Positive ions
Fluorescence
Thermodynamics

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry
  • Atomic and Molecular Physics, and Optics
  • Instrumentation
  • Spectroscopy

Cite this

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abstract = "The mechanism of interaction of ondansetron hydrochloride (OND) to serum albumins [bovine serum albumin (BSA) and human serum albumin (HSA)] was studied for the first time employing fluorimetric, circular dichroism, FTIR and UV-vis absorption techniques under the simulated physiological conditions. Fluorimetric results were utilized to investigate the binding and conformational characteristics of protein upon interaction with varying concentrations of the drug. Higher binding constant values revealed the strong interaction between the drug and protein while the number of binding sites close to unity indicated single class of binding site for OND in protein. Thermodynamic results revealed that both hydrogen bond and hydrophobic interactions played a major role in stabilizing drug-protein complex. Site marker competitive experiments indicated that the OND bound to albumins at subdomin II A (Sudlow's site I). Further, the binding distance between OND and serum albumin was calculated based on the F{\"o}rster's theory of non-radioactive energy transfer and found to be 2.30 and 3.41 nm, respectively for OND-BSA and OND-HSA. The circular dichroism data revealed that the presence of OND decreased the α-helix content of serum albumins. 3D-fluorescence results also indicated the conformational changes in protein upon interaction with OND. Further, the effects of some cations have been investigated in the interaction of drug to protein.",
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Exploring the binding mechanism of ondansetron hydrochloride to serum albumins : Spectroscopic approach. / Sandhya, B.; Hegde, Ashwini H.; Ramesh, K. C.; Seetharamappa, J.

In: Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy, Vol. 86, 01.02.2012, p. 410-416.

Research output: Contribution to journalArticle

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