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Influence of assembling pH on the stability of poly(L-glutamic acid) and poly(L-lysine) multilayers against urea treatment
Authors:Zhou Jie  Wang Bo  Tong Weijun  Maltseva Elena  Zhang Gang  Krastev Rumen  Gao Changyou  Möhwald Helmuth  Shen Jiacong
Institution:Key Laboratory of Macromolecular Synthesis and Functionalization, Ministry of Education, Department of Polymer Science and Engineering, Zhejiang University, Hangzhou 310027, China.
Abstract:Polyelectrolyte multilayers of poly(L-glutamic acid) (PGA) and poly(L-lysine) (PLL) were built up using the layer-by-layer (LbL) technique in low pH (3.6, PM3.6) and in neutral pH (7.4, PM7.4) solutions. The multilayers were then treated with a concentrated urea (one kind of denaturant for proteins and polypeptides) solution (8M) and rinsed with corresponding buffer. The buildup and treatment processes were investigated by ultraviolet visible spectroscopy and ellipsometry. The surface morphology was observed by scanning force microscopy (SFM). The inner structures were determined by X-ray reflectometry and circular dichroism spectroscopy (CD). An exponential growth of the optical mass and the layer thickness was observed for both PM3.6 and PM7.4. After urea treatment, a significant mass loss for PM3.6 was found, while no mass change was recorded for PM7.4. The dominant driving force for PM7.4 is electrostatic interaction, resulting in multilayers with an abundant beta-sheet structure, which has higher stability against urea treatment. By contrast, the dominant driving force for PM3.6 is hydrogen bonding and hydrophobic interaction, which are sensitive to the urea treatment. The mechanism is substantiated by molecular mechanics calculation. This has offered a convenient pathway to mediate the multilayer properties, which is of great importance for potential applications.
Keywords:Polypeptide  Multilayer  Stability  Hydrogen bonding  Electron interaction
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