Dynamic surface activity by folding and unfolding an amphiphilic alpha-helix
We describe a rationally designed peptide with tunable surface activity, where the dynamics of surface activity are an outcome of helical folding. Our rationally designed model peptide is surface-active only as an alpha-helix. We apply circular dichroism to show that the folded population can be con...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 24(2008), 18 vom: 16. Sept., Seite 9923-8 |
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| Weitere Verfasser: | , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2008
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Ligands Peptides Proteins Surface-Active Agents Water 059QF0KO0R DNA |
| Zusammenfassung: | We describe a rationally designed peptide with tunable surface activity, where the dynamics of surface activity are an outcome of helical folding. Our rationally designed model peptide is surface-active only as an alpha-helix. We apply circular dichroism to show that the folded population can be controlled with changes in electrolyte concentration, and we apply pendant bubble tensiometry to explore dynamic surfactant activity. This study shows a peptide that responds to environmental stimuli with dynamic folding and surface activity. Extending this concept to selective binding peptides will lead to new tools, where dynamic surface activity is coupled to targeted binding |
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| Beschreibung: | Date Completed 17.10.2008 Date Revised 22.03.2024 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/la801695j |