Abstract：
:The interaction between ovalbumin (OVA) and three purine alkaloids (caffeine, theophylline and diprophylline) was investigated by the aid of intrinsic and synchronous fluorescence, ultraviolet-vis absorbance, resonance light-scattering spectra and three-dimensional fluorescence spectra techniques. Results showed that the formation of complexes gave rise to the fluorescence quenching of OVA by caffeine, theophylline, and diprophylline. Static quenching was confirmed to results in the fluorescence quenching. The binding site number n, apparent binding constant KA and corresponding thermodynamic parameters were measured at different temperatures. The binding process was spontaneous molecular interaction procedures in which both enthalpy and Gibbs free energy decreased. Van der Waals forces and hydrogen bond played a major role in stabilizing the complex. The comparison between caffeine, theophylline, and diprophylline was made, and thermodynamic results showed that diprophylline was the strongest quencher and bound to OVA with the highest affinity among three compounds. The influence of molecular structure on the binding aspects was reported.
journal_name
Mol Biol Repjournal_title
Molecular biology reportsauthors
Wang RQ,Yin YJ,Li H,Wang Y,Pu JJ,Wang R,Dou HJ,Song CJ,Wang RYdoi
10.1007/s11033-012-2418-xsubject
Has Abstractpub_date
2013-04-01 00:00:00pages
3409-18issue
4eissn
0301-4851issn
1573-4978journal_volume
40pub_type
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