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Predict more albumin - ligand interactions now!

1. Luminescence. 2012 Apr 12. doi: 10.1002/bio.2364. [Epub ahead of print]

Study of the interaction between sodium salts of
(2E)-3-(4'-halophenyl)prop-2-enoyl sulfachloropyrazine and bovine serum albumin
by fluorescence spectroscopy.

Luo X, Du C, Wei J, Deng J, Lin Y, Lin C.

School of Chemistry and Chemical Engineering, Guangxi University, Nanning,
Guangxi, 530004, People's Republic of China.

Three sodium salts of (2E)-3-(4'-halophenyl)prop-2-enoyl sulfachloropyrazine
(CCSCP) were synthesized and their structures were determined by (1) H and (13) C
NMR, LC-MS and IR. The binding properties between CCSCPs and bovine serum albumin
(BSA) were studied using fluorescence spectroscopy in combination with UV-vis
absorbance spectroscopy. The results indicate that the fluorescence quenching
mechanisms between BSA and CCSCPs were static quenching at low concentrations of
CCSCPs or combined quenching (static and dynamic) at higher CCSCP concentrations
of 298, 303 and 308 K. The binding constants, binding sites and corresponding
thermodynamic parameters (ΔH, ΔS, ΔG) were calculated at different temperatures.
All ΔG values were negative, which revealed that the binding processes were
spontaneous. Although all CCSCPs had negative ΔH and positive ΔS, the
contributions of ΔH and ΔS to ΔG values were different. When the 4'-substituent
was fluorine or chlorine, van der Waals interactions and hydrogen bonds were the
main interaction forces. However, when the halogen was bromine, ionic interaction
and proton transfer controlled the overall energetics. The binding distances
between CCSCPs and BSA were determined using the Förster non-radiation energy
transfer theory and the effects of CCSCPs on the conformation of BSA were
analyzed by synchronous fluorescence spectroscopy. Copyright © 2012 John Wiley &
Sons, Ltd.

Copyright © 2012 John Wiley & Sons, Ltd.

PMID: 22496074 [PubMed - as supplied by publisher]