Abstract
The interaction between glyoxal-bis-(2-hydroxyanil) (GBH) and bovine serum albumin (BSA) was studied by spectroscopic methods including fluorescence spectroscopy, circular dichroism (CD) and UV–visible absorption spectra. The mechanism for quenching the fluorescence of BSA by GBH is discussed. The number of binding sites n and observed binding constant K b were measured by the fluorescence quenching method. The thermodynamic parameters ΔH θ, ΔG θ, and ΔS θ were calculated at different temperatures and the results indicate that hydrogen bonding and van der Waals forces played major roles in the reaction. The distance r between the donor (BSA) and acceptor (GBH) molecules was obtained according to Förster’s theory of non-radiation energy transfer. Synchronous fluorescence and three-dimensional fluorescence spectra were used to investigate the structural change of BSA molecules that occur upon addition of GBH, and these results indicate that the secondary structure of BSA molecules is changed by the presence of GBH.
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Zhang, HX., Huang, X., Mei, P. et al. Interaction between Glyoxal-bis-(2-hydroxyanil) and Bovine Serum Albumin in Solution. J Solution Chem 37, 631–640 (2008). https://doi.org/10.1007/s10953-008-9268-0
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DOI: https://doi.org/10.1007/s10953-008-9268-0