| 초록 |
Herein, we investigated interfacial behaviors of elastin-like polypeptide (ELP), an artificial biopolymer based on VPGXG (X is any amino acid except Proline) pentapeptide repeats, as a function of temperature. The compression surface pressure-area (π-A) isotherms and the deposition onto mica substrates were performed under variable subphase conditions using Langmuir-Blodgett (LB) technique. The surface morphologies of the LB monolayers were subsequently imaged using atomic force microscopy. Amphiphilic ELP formed a stable monolayer at the air-water interface. The increase in water subphase temperature was translated into overall shift of the π-A isotherms toward lager interfacial areas. This change is associated with the thermoresponsive interfacial behaviors of ELP such as conformational transitions occurring around the lower critical solution temperature and intermolecular interactions which lead to distinctive aggregate formation at the interface during compression. |
