Probing the Interaction Between a Surfactant-Cobalt(III) Complex and Bovine Serum Albumin

Senthil Kumar, Rajendran ; vanden Bergh, Hubert ; Wagnières, Georges

In: Journal of Solution Chemistry, 2012, vol. 41, no. 2, p. 294-306

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    Summary
    The mechanism of binding of the surfactant-cobalt(III) complex, cis-[Co(phen)2(C14H29NH2)Cl](ClO4)2⋅3H2O (phen = 1,10-phenanthroline, C14H29NH2 = tetradecylamine) with bovine serum albumin (BSA) was investigated by UV-vis absorption, circular dichroism (CD) and fluorescence spectroscopic techniques. The results of fluorescence titration revealed that the surfactant-cobalt(III) complex quenched the intrinsic fluorescence of BSA through a combination of static and dynamic quenching. The apparent binding constant (K a) and number of binding sites (n) were calculated below and above the critical micelle concentration (CMC). The thermodynamic parameters determined by the van't Hoff analysis of the constants (ΔH ∘=14.87 kJ⋅mol−1; ΔS ∘=152.88 J⋅mol−1⋅K−1 below the CMC and 25.70 kJ⋅mol−1 and 243.14 J⋅mol−1⋅K−1, respectively, above the CMC) clearly indicate that the binding is entropy-driven and enthalpically disfavored. Based on Förster's theory of non-radiation energy transfer, the binding distance, r, between donor (BSA) and the acceptor (surfactant-cobalt(III) complex) was evaluated. UV-vis, CD and synchronous fluorescence spectral results showed that the binding of the surfactant-cobalt(III) complex to BSA induced conformational changes in BSA