Analytical investigation of the influence of ornidazole on the native protein fluorescence

Spectrochim Acta A Mol Biomol Spectrosc. 2018 Aug 5:201:178-184. doi: 10.1016/j.saa.2018.05.003. Epub 2018 May 3.

Abstract

A novel spectrofluorimetric method for the determination of ornidazole (ORN) in pure form and dosage forms was developed based on the influence of ORN on the native fluorescence of bovine serum albumin (BSA) in a stimulated physiological environment. The obtained data reveal that the presence of ORN has a strong quenching effect on the fluorescence of BSA through both a dynamic and a static process. The parameters of the binding of ORN to BSA were calculated at different temperatures. Thermodynamic parameters values suggest a role of electrostatic and hydrophobic forces in the binding of ORN to BSA. The investigated method for the determination of ORN is accurate, precise and sensitive with a detection limit of 0.106 μg/mL and a quantification limit of 0.353 μg/mL. The quenching method was applied successfully in the determination of ORN in pure form and dosage forms.

Keywords: Combine quenching process; Ornidazole; Serum albumin; Tyrosine.

MeSH terms

  • Hydrophobic and Hydrophilic Interactions
  • Limit of Detection
  • Linear Models
  • Ornidazole / chemistry*
  • Ornidazole / metabolism
  • Protein Binding
  • Reproducibility of Results
  • Serum Albumin, Bovine / analysis*
  • Serum Albumin, Bovine / chemistry*
  • Serum Albumin, Bovine / metabolism
  • Spectrometry, Fluorescence / methods*
  • Thermodynamics
  • Tyrosine / chemistry

Substances

  • Serum Albumin, Bovine
  • Tyrosine
  • Ornidazole