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Biophysical studies of the interaction between a triazole derivative and bovine serum albumin by multi-spectroscopic and molecular modeling methods

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Abstract

The interaction between 3-thiol-4-(2,4-dichlorobenzylideneamino)-5-methyl-4H-1,2,4-triazole (CBTZ) and bovine serum albumin (BSA) under physiological conditions was investigated by fluorescence, UV-vis absorption and circular dichroism (CD) spectroscopy as well as molecular modeling methods. The result of fluorescence experiment indicates the static quenching as a result of the formation of the CBTZ-BSA complex. The binding constants (K a) at different temperatures were calculated according to the modified Stern-Volmer equation. The enthalpy change (ΔH) and entropy change (ΔS) were determined based on the van’t Hoff equation. Both negative ΔH and ΔS indicated that van der Waals and hydrogen-bonding forces were the dominant intermolecular forces to stabilize the CBTZ-BSA complex. Site marker competitive replacement experiments demonstrated that binding of CBTZ to BSA primarily took place in sub-domain IIA (Sudlow’s site I). The binding distance (r = 7.2 nm) between CBTZ and the tryptophan residue of BSA was estimated according to the theory of fluorescence resonance energy transfer (FRET). The conformational studies by circular dichroism (CD) and three-dimensional fluorescence spectroscopy showed that the presence of CBTZ induced minor changes of the secondary structure of BSA. Molecular modeling study further confirmed the binding mode obtained experimentally.

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Correspondence to FengLei Jiang.

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Fu, J., Wang, K., Ge, Y. et al. Biophysical studies of the interaction between a triazole derivative and bovine serum albumin by multi-spectroscopic and molecular modeling methods. Sci. China Chem. 54, 788–796 (2011). https://doi.org/10.1007/s11426-011-4260-8

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  • DOI: https://doi.org/10.1007/s11426-011-4260-8

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