Binding of several benzodiazepines to bovine serum albumin: Fluorescence study.
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.
Machicote
Roberta G
RG
División Química Analítica, Departamento de Química, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, Calle 47 y 115, 1900 La Plata, Argentina. rmachicote@quimica.unlp.edu.ar
Pacheco
María E
ME
Bruzzone
Liliana
L
D000818:Animals; D001569:Benzodiazepines / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D002417:Cattle; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods; D015394:Molecular Structure; D011485:Protein Binding; D011487:Protein Conformation; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism*; D013050:Spectrometry, Fluorescence / Q000379:methods; D013816:Thermodynamics
D001569:Benzodiazepines; D012710:Serum Albumin, Bovine