Switchable wettability on cooperative dual-responsive poly-L-lysine surface
A cooperative dual-responsive polypeptide surface switching between superhydrophilic and superhydrophobic states is presented. This macroscopic phenomenon of surface originates from the combination of the cooperative unfolding/aggregation of the poly-L-lysine (PLL) immobilized on the substrate with...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 26(2010), 2 vom: 19. Jan., Seite 1024-8 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2010
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Polylysine 25104-18-1 |
| Zusammenfassung: | A cooperative dual-responsive polypeptide surface switching between superhydrophilic and superhydrophobic states is presented. This macroscopic phenomenon of surface originates from the combination of the cooperative unfolding/aggregation of the poly-L-lysine (PLL) immobilized on the substrate with micro/nanocomposite structure in response to pH and temperature. At pH lower than the pK(a) of PLL (approximately 11.0), PLL mainly adopts a random coil conformation, which corresponds to the superhydrophilic state on the rough surface substrate. Raising the pH to higher than the pK(a) allows the appearance of alpha-helix conformation, which also corresponds to the hydrophilic state. However, heating up the surface at pH higher than the pK(a) destabilizes the alpha-helix conformation and induces the formation of aggregated beta-sheet structures, which represents the superhydrophobic state. Lowering the pH and temperature simultaneously switches a reversible conversion from superhydrophobic to superhydrophilic states. In the switching process, the hydrophobicity and hydrophilicity can be "memorized" due to the cooperative pH and temperature stimuli-induced unfolding/aggregation behaviors of PLL. This provides a new exciting prospect for understanding surface properties of polypeptides and the design of smart material surfaces with potential applications in nanodevices, bioseparation, and biosensors |
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| Beschreibung: | Date Completed 11.03.2010 Date Revised 13.01.2010 published: Print Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/la9041452 |