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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 28, Number 5
BKCSDE 28(5)
May 20, 2007 

Thermodynamic and Structural Studies on the Human Serum Albumin in the Presence of a Polyoxometalate
D. Ajloo, H. Behnam, A. A. Saboury, F. Mohamadi-Zonoz, B. Ranjbar, A. A. Moosavi-Movahedi, Z. Hasani, K. Alizadeh, M. Gharanfoli, M. Amani
Polyoxometalate, Human serum albumin, Isothermal titration calorimetery, Circular dichroism, Fluorescence
The interaction of a polyoxometal (POM), K6SiW11Co(H2O)O39.10H2O (K6) as a Keggin, with human serum albumin (HSA) was studied by different methods and techniques. Binding studies show two sets of binding sites for interaction of POM to HSA. Binding analysis and isothermal calorimetery revealed that, the first set of binding site has lower number of bound ligand per mole of protein (ν), lower Hill constant (n), higher binding constant (K), more negative entropy (ΔS) and more electrostatic interaction in comparison to the second set of binding site. In addition, differential scanning calorimetery (DSC) and spectrophotometery data showed that, there are two energetic domains. The first domain is less stable (lower Tm and Cp) which corresponds to the tail segment of HSA and another with more stability is related to the head segment of HSA. Polyoxometal also decreases the stability of protein as Tm, secondary and tertiary structure as well as quenching of the fluorescence decrease. On other hand, perturbations in tertiary structure are more than secondary structure.
730 - 736
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