Study on the binding of 2,3-diazabicyclo[2.2.2]oct-2-ene with bovine serum albumin by fluorescence spectroscopy

The interaction of 2,3-diazabicyclo[2.2.2]oct-2-ene (DBO) with bovine serum albumin (BSA) has been studied using absorption and steady state fluorescence techniques. Fluorescence spectrum of BSA (λexi=280 nm) in the presence of DBO clearly shows that DBO acts as a quencher. The number of binding sites 'n' and apparent binding constant 'K' were measured by Stern-Volmer equation. Synchronous fluorescence and absorption spectra were used to study protein conformation. The interaction between DBO and BSA is consistent with static quenching and the conformational changes of BSA observed.