Anionic branched surfactants as alternative denaturing agents for protein separations
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...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1985. - 30(2014), 5 vom: 11. Feb., Seite 1351-60 |
|---|---|
| 1. Verfasser: | |
| Weitere Verfasser: | |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2014
|
| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, U.S. Gov't, Non-P.H.S. Anions Proteins Surface-Active Agents Sodium Dodecyl Sulfate 368GB5141J |
| Zusammenfassung: | 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 |
|---|---|
| Beschreibung: | Date Completed 21.10.2014 Date Revised 11.02.2014 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/la404392t |