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Analysis of Binding Interaction between Bovine Serum Albumin and the Cobalt(II) Complex with Salicylaldehyde-2-phenylquinoline-4-carboylhydrazone
- Source :
- Chemical and Pharmaceutical Bulletin. 57:1237-1242
- Publication Year :
- 2009
- Publisher :
- Pharmaceutical Society of Japan, 2009.
-
Abstract
- The interaction between bovine serum albumin (BSA) and the cobalt(II) complex with salicylaldehyde-2-phenylquinoline-4-carboylhydrazone (Co-SPC) was investigated using fluorescence spectroscopy, UV absorption, and circular dichroism (CD) under simulated physiologic conditions for the first time. Fluorescence data and UV absorption spectra revealed that the intrinsic fluorescence of BSA was strongly quenched by Co-SPC in terms of a static quenching process at a lower concentration of the complex and a combined quenching process at a higher concentration of the complex. Binding constants and binding sites were evaluated. The average binding distance between Co-SPC and BSA was obtained (2.28 nm) on the basis of Förster's theory. The thermodynamic parameters indicated that hydrophobic force played a major role in the binding. The binding of Co-SPC to BSA leads to changes in the conformation of BSA according to synchronous fluorescence spectra and CD data.
- Subjects :
- Circular dichroism
chemistry.chemical_element
Fluorescence
Fluorescence spectroscopy
Structure-Activity Relationship
chemistry.chemical_compound
Drug Discovery
Organometallic Compounds
Animals
Bovine serum albumin
Binding site
Binding Sites
Quenching (fluorescence)
biology
Circular Dichroism
Hydrazones
Serum Albumin, Bovine
Cobalt
General Chemistry
General Medicine
Crystallography
Spectrometry, Fluorescence
Energy Transfer
chemistry
Salicylaldehyde
Quinolines
biology.protein
Cattle
Spectrophotometry, Ultraviolet
Subjects
Details
- ISSN :
- 13475223 and 00092363
- Volume :
- 57
- Database :
- OpenAIRE
- Journal :
- Chemical and Pharmaceutical Bulletin
- Accession number :
- edsair.doi.dedup.....8d554d4bd73658eeb4b010aa81483606