Effect of urea on bovine serum albumin in aqueous and reverse micelle environments investigated by small angle X-ray scattering, fluorescence and circular dichroism
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Sociedade Brasileira de Física
2004
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| author | Rosangela Itri |
| author_facet | Rosangela Itri |
| contents | Effect of urea on bovine serum albumin in aqueous and reverse micelle environments investigated by small angle X-ray scattering, fluorescence and circular dichroism Rosangela Itri Wilker Caetano Leandro R. S. Barbosa Mauricio S. Baptista Física, Astronomía y Matemáticas The influence that urea has on the conformation of water-soluble globular protein, bovine serum albumin (BSA),exposed directly to the aqueous solution as compared to the condition where the macromolecule is confined inthe Aerosol-OT (AOT - sodium bis-2-ethylhexyl sulfosuccinate)/n-hexane/water reverse micelle (RM) is addressed.Small angle X-ray scattering (SAXS), tryptophan (Trp) fluorescence emission and circular dichroism(CD) spectra of aqueous BSA solution in the absence and in the presence of urea (3M and 5M) confirm theknown denaturating effect of urea in proteins. The loss of the globular native structure is observed by theincrease in the protein maximum dimension and gyration radius, through the Trp emission increase and maximumred-shift as well as the decrease in ®-helix content. In RMs, the Trp fluorescence and CD spectra showthat BSA is mainly located in its interfacial region independently of the micellar size. Addition of urea in thisBSA/RM system also causes changes in the Trp fluorescence (emission decrease and maximum red-shift) andin the BSA CD spectra (decrease in ®-helix content), which are compatible with the denaturation of the proteinand Trp exposition to a more apolar environment in the RM. The fact that urea causes changes in the proteinstructure when it is located in the interfacial region (evidenced by CD) is interpreted as an indication that thedirect interaction of urea with the protein is the major factor to explain its denaturating effect. 2004 artículo científico 0103-9733 https://www.redalyc.org/articulo.oa?id=46434108 en http://www.redalyc.org/revista.oa?id=464 Brazilian Journal of Physics application/pdf Sociedade Brasileira de Física Brazilian Journal of Physics (Brasil) Num.1 Vol.34 |
| format | Artículo científico |
| id | redalyc_46434108 |
| institution | Redalyc |
| language | en |
| publishDate | 2004 |
| publisher | Sociedade Brasileira de Física |
| spellingShingle | Effect of urea on bovine serum albumin in aqueous and reverse micelle environments investigated by small angle X-ray scattering, fluorescence and circular dichroism Rosangela Itri Física, Astronomía y Matemáticas Effect of urea on bovine serum albumin in aqueous and reverse micelle environments investigated by small angle X-ray scattering, fluorescence and circular dichroism Rosangela Itri Wilker Caetano Leandro R. S. Barbosa Mauricio S. Baptista Física, Astronomía y Matemáticas The influence that urea has on the conformation of water-soluble globular protein, bovine serum albumin (BSA),exposed directly to the aqueous solution as compared to the condition where the macromolecule is confined inthe Aerosol-OT (AOT - sodium bis-2-ethylhexyl sulfosuccinate)/n-hexane/water reverse micelle (RM) is addressed.Small angle X-ray scattering (SAXS), tryptophan (Trp) fluorescence emission and circular dichroism(CD) spectra of aqueous BSA solution in the absence and in the presence of urea (3M and 5M) confirm theknown denaturating effect of urea in proteins. The loss of the globular native structure is observed by theincrease in the protein maximum dimension and gyration radius, through the Trp emission increase and maximumred-shift as well as the decrease in ®-helix content. In RMs, the Trp fluorescence and CD spectra showthat BSA is mainly located in its interfacial region independently of the micellar size. Addition of urea in thisBSA/RM system also causes changes in the Trp fluorescence (emission decrease and maximum red-shift) andin the BSA CD spectra (decrease in ®-helix content), which are compatible with the denaturation of the proteinand Trp exposition to a more apolar environment in the RM. The fact that urea causes changes in the proteinstructure when it is located in the interfacial region (evidenced by CD) is interpreted as an indication that thedirect interaction of urea with the protein is the major factor to explain its denaturating effect. 2004 artículo científico 0103-9733 https://www.redalyc.org/articulo.oa?id=46434108 en http://www.redalyc.org/revista.oa?id=464 Brazilian Journal of Physics application/pdf Sociedade Brasileira de Física Brazilian Journal of Physics (Brasil) Num.1 Vol.34 |
| title | Effect of urea on bovine serum albumin in aqueous and reverse micelle environments investigated by small angle X-ray scattering, fluorescence and circular dichroism |
| topic | Física, Astronomía y Matemáticas |
| url | https://www.redalyc.org/articulo.oa?id=46434108 |