Binding of several benzodiazepines to bovine serum albumin: Fluorescence study

Spectrochim Acta A Mol Biomol Spectrosc. 2010 Oct 1;77(2):466-72. doi: 10.1016/j.saa.2010.06.020. Epub 2010 Jun 19.

Abstract

The interactions of lorazepam, oxazepam and bromazepam with bovine serum albumin (BSA) were studied by fluorescence spectrometry. The Stern-Volmer quenching constants and corresponding thermodynamic parameters DeltaH, DeltaG and DeltaS were calculated. The binding constants and the number of binding sites were also investigated. The distances between the donor (BSA) and the acceptors (benzodiazepines) were obtained according to fluorescence resonance energy transfer and conformational changes of BSA were observed from synchronous fluorescence spectra.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Benzodiazepines / chemistry*
  • Benzodiazepines / metabolism*
  • Binding Sites
  • Cattle
  • Fluorescence Resonance Energy Transfer / methods
  • Molecular Structure
  • Protein Binding
  • Protein Conformation
  • Serum Albumin, Bovine / chemistry*
  • Serum Albumin, Bovine / metabolism*
  • Spectrometry, Fluorescence / methods
  • Thermodynamics

Substances

  • Benzodiazepines
  • Serum Albumin, Bovine