title

مطالعات ترمودینامیکی و ساختاری آبومین انسانی در حضور پلی اکسومتالات

عاجلو, داوود and بهنام, حسین and صبوری, علی اکبر and محمدی زنوزی, فرخزاد and رنجبر, بیژن and موسوی موحدی, علی اکبر and حسنی, زهرا and علیزاده, کمال and قرنفولی, محسن and امانی, مجتبی (1386) مطالعات ترمودینامیکی و ساختاری آبومین انسانی در حضور پلی اکسومتالات. Bulletin of the Korean Chemical Society ــ 28 (5). pp. 730-736. شاپا 0253-2964

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Title

Thermodynamic and structural studies on the human serum albumin in the presence of a polyoxometalate

English Abstract

The interaction of a polyoxometal (POM), K<sub>6</sub>SiW <sub>11</sub>Co(H<sub>2</sub>O)O<sub>39</sub>.10H<sub>2</sub>O (K<sub>6</sub>) 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 (�S) 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 T<sub>m</sub> and C<sub>p</sub>) 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 T<sub>m</sub>, secondary and tertiary structure as well as quenching of the fluorescence decrease. On other hand, perturbations in tertiary structure are more than secondary structure

Item Type:Article
زبان سند : انگلیسی
نویسنده مسئول :داوود عاجلو
Additional Information:cited By (since 1996) 6
کلیدواژه ها (انگلیسی):Blood; Coulomb interactions; Differential scanning calorimetry; Fluorescence; Molecular structure; Perturbation techniques; Thermodynamics, Circular dichroisms; Human serum albumin (HSA); Isothermal titration calorimetery; Polyoxometalate, Proteins
Subjects:QU Biochemistry
Divisions:Faculty of Medicine > Department of Basic Sciences > Department of Biophysics
ID Code:1064
Deposited By: MS Soghra Golmaghani
Deposited On:13 Dec 1388 06:29
Last Modified:20 Jan 1393 13:06

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