ArticleMolecular biology reports2011
Studies on the interaction between benzophenone and bovine serum albumin by spectroscopic methods.
Article in Molecular biology reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 33 citations in OpenAlex.
- Protein-polymer conjugation via ligand affinity and photoactivation of glutathione S-transferase.Bioconjugate chemistry · 2014Article
- Systematic investigation of interactions between papain and MPA-capped CdTe quantum dots.Molecular biology reports · 2013Article
- Characterization of the binding of metoprolol tartrate and guaifenesin drugs to human serum albumin and human hemoglobin proteins by fluorescence and circular dichroism spectroscopy.Journal of fluorescence · 2013Article
- Toxicity of CdTe QDs with different sizes targeted to HSA investigated by two electrochemical methods.Molecular biology reports · 2013Article
- The binding characteristics of the interaction between 3-(2-cyanoethyl) cytosine and human serum albumin.Molecular biology reports · 2012Article
- Interaction of ergosterol with bovine serum albumin and human serum albumin by spectroscopic analysis.Molecular biology reports · 2012Article
- Study on the interaction between isoniazid and bovine serum albumin by fluorescence spectroscopy: the effect of dimethylsulfoxide.Molecular biology reports · 2012Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The interaction between benzophenone (BP) and bovine serum albumin (BSA) was investigated by the methods of fluorescence spectroscopy combined with UV-Vis absorption and circular dichroism (CD) measurements under simulative physiological conditions. The experiment results showed that the fluorescence quenching of BSA by BP was resulted from the formation of a BP-BSA complex and the corresponding association constants (Ka) between BP and BSA at four different temperatures had been determined using the modified Stern-Volmer equation. The enthalpy change (ΔH) and entropy change (ΔS) were calculated to be -43.73 kJ mol(-1) and -53.05 J mol(-1) K(-1), respectively, which suggested that hydrogen bond and van der Waals force played major roles in stabilizing the BP-BSA complex. Site marker competitive experiments indicated that the binding of BP to BSA primarily took place in site I (sub-domain IIA). The conformational investigation showed that the presence of BP decreased the α-helical content of BSA and induced the slight unfolding of the polypeptides of protein, which confirmed some micro-environmental and conformational changes of BSA molecules.
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