Effect of salts and sodium dodecyl sulfate on chaperone activity of camel αS1-CN: Insulin as the target protein
| Autor: | Jalil Badraghi, Ali Akbar Saboury, Ahmad Sharifzadeh, Reza Yousefi, Thomas Haertlé, Ali Akbar Moosavi-Movahedi, Faizan Ahmad |
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| Přispěvatelé: | Institute of Biochemistry and Biophysics, Pawinskiego 5a, Shahid Beheshti University, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Jamia Millia Islamia University, Partenaires INRAE, Foundation for Advancement of Science and Technology in Iran |
| Rok vydání: | 2009 |
| Předmět: |
endocrine system
Camelus medicine.medical_treatment SALTS Anilino Naphthalenesulfonates Fluorescence chemistry.chemical_compound Colloid and Surface Chemistry Pulmonary surfactant DEHYDRATION Casein medicine Animals SELS Dehydration Physical and Theoretical Chemistry Chaperone activity Sodium dodecyl sulfate Protein Structure Quaternary SDS Chromatography biology Chemistry Insulin Caseins Sodium Dodecyl Sulfate CAMEL ALPHA S1-CASEIN Surfaces and Interfaces General Medicine AGGREGATION medicine.disease INSULIN HYDROPHOBIC TAIL SURFACTANT DODECYL SULFATE SODIUM Dithiothreitol Biochemistry Chaperone (protein) biology.protein Cattle CHAPERONE-LIKE PROPERTIES Target protein SITE HYDROPHOBE [CHIM.OTHE]Chemical Sciences/Other Hydrophobic and Hydrophilic Interactions CHAPERON MOLECULAIRE Molecular Chaperones Biotechnology |
| Zdroj: | Colloids and Surfaces B: Biointerfaces Colloids and Surfaces B: Biointerfaces, Elsevier, 2009, 71 (2), pp.300-305. ⟨10.1016/j.colsurfb.2009.03.008⟩ |
| ISSN: | 0927-7765 |
| DOI: | 10.1016/j.colsurfb.2009.03.008 |
| Popis: | In this study camel [alpha]S1-casein ([alpha]S1-CN) was purified, using a two-step purification procedure. The anti-aggregation (chaperone-like) ability of the purified protein sample was examined in a wide range of experimental conditions and at different concentrations of camel [alpha]S1-CN, in the presence of salts and sodium dodecyl sulfate (SDS). To examine chaperone-like activity of camel [alpha]S1-CN, bovine pancreatic insulin was used as the target protein. Insulin aggregation performed chemically in the presence of 20 mM dithiotreitol (DTT) and was studied at 360 nm wavelength by UV-vis spectrophotometer. Camel [alpha]S1-CN exhibited a dose-dependent chaperone-like activity as the molar ratios of chaperone/target protein varied between 0-0.07. The presence of salts or surfactants changing the protein properties had an influence on chaperone capacity of camel [alpha]S1-CN. The results of UV- visible and fluorimetric measurements indicated that the salts neutralize the chaperone-like activity of casein due to dehydration effect and the increased association and aggregation of proteins, while SDS plays a role as chaperone and chaperone-like properties of camel [alpha]S1-CN enhanced in the presence of SDS due to the binding of the hydrophobic tail of SDS and [alpha]S1-CN to the exposed hydrophobic sites of insulin strongly preventing aggregation of insulin. |
| Databáze: | OpenAIRE |
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