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Binding Studies of a Schiff Base Compound Containing a 1,2,4‐Triazole Ring with Bovine Serum Albumin Using Spectroscopic Methods
Author(s) -
Mei Ping,
Liu Yang,
Zhang Yezhong,
Fu Jiaxin,
Sun Xiaohong,
Liu Yi
Publication year - 2010
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.201090319
Subject(s) - chemistry , bovine serum albumin , circular dichroism , hydrogen bond , schiff base , quenching (fluorescence) , triazole , molecule , fluorescence spectroscopy , enthalpy , fluorescence , crystallography , stereochemistry , chromatography , organic chemistry , physics , quantum mechanics
The binding interaction of a Schiff base compound containing a 1,2,4‐triazole ring [4‐(4‐chlorobenzyl‐ideneamino)‐5‐methyl‐1,2,4‐triazole‐3‐thiol, CTT] with bovine serum albumin (BSA) was studied by spectroscopy methods including fluorescence and circular dichroism spectrum under simulative physiological conditions. Fluorescence investigation revealed that the fluorescence quenching of BSA was induced by the formation of a relative stable CTT‐BSA complex. The corresponding binding constants ( K a ) between CTT and BSA at three different temperatures were calculated according to the modified Stern‐Volmer equation. The enthalpy change (Δ H ⊖ ) and entropy change (Δ S ⊖ ) were calculated to be −15.78 kJ·mol −1 and 49.23 J·mol −1 ·K −1 , respectively, which suggested that hydrophobic forces and hydrogen bond played major roles in stabilizing the CTT‐BSA complex. Site marker competitive experiments indicated that the binding of CTT to BSA primarily took place in sub‐domain IIIA (site II) of BSA. The binding distance ( r ) between CTT and the tryptophan residue of BSA was obtained to be 4.3 nm based on F?rster theory of non‐radioactive energy transfer. The conformational investigation revealed that the presence of CTT decreased the α ‐helix content of BSA (from 58.62% to 54.66%) and induced the slight unfolding of the polypeptides of protein, which confirmed some micro‐environmental and conformational changes of BSA molecules.