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231224s2014 xx |||||o 00| ||eng c |
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|a 10.1021/la404392t
|2 doi
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|a eng
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|a Ospinal-Jiménez, Mónica
|e verfasserin
|4 aut
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|a Anionic branched surfactants as alternative denaturing agents for protein separations
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|c 2014
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|a Date Completed 21.10.2014
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|a Date Revised 11.02.2014
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Denaturation of a group of model proteins of diverse size and composition with three branched alkyl surfactants-sodium 2-ethylhexyl sulfate (2-EHS), sodium 3,7-dimethyloctyl sulfate (3,7-DMOS), and sodium 2-butyloctyl sulfate (2-BOS)-has been investigated using circular dichroism (CD), small-angle X-ray scattering, and polyacrylamide gel electrophoresis (PAGE). Circular dichroism reveals that 2-BOS disrupts to a higher extent the secondary structure for most of the proteins. Also, it is found that upon adsorption the shape of the protein-surfactant complexes varies from "pearl necklace" to ellipsoidal depending on the surfactant that is used. Macroscopic separations also reveal that branching sodium alkyl sulfates with n-butyl (2-BOS) and n-methyl (3,7-DMOS) groups significantly affects their performance in PAGE. 3,7-DMOS and 2-BOS result in anomalous migrations that deviate from the expected electrophoretic mobility. A combined interpretation of spectroscopy, scattering, and polyacrylamide gel electrophoresis suggests that 2-BOS promotes stronger modification of proteins during denaturation. The findings in this work aim to improve protein electrophoretic separations and the design of novel surfactants
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|a Journal Article
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|a Research Support, U.S. Gov't, Non-P.H.S.
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|a Anions
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|a Proteins
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|a Surface-Active Agents
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|a Sodium Dodecyl Sulfate
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|a Pozzo, Danilo C
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1985
|g 30(2014), 5 vom: 11. Feb., Seite 1351-60
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|g volume:30
|g year:2014
|g number:5
|g day:11
|g month:02
|g pages:1351-60
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|u http://dx.doi.org/10.1021/la404392t
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