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Effects of γ-Zein Peptides on Lipid Membrane Organization: Quartz Crystal Microbalance with Dissipation and Langmuir Monolayer Studies
- Zou, Yuan, Pan, Runting, Liu, Yingli, Liu, Xiao, Chen, Xiaowei, Wang, Jing, Wan, Zhili, Guo, Jian, Yang, Xiaoquan
- Colloids and surfaces 2019
- atomic force microscopy, binding capacity, cell membranes, fluorescence, gamma-zein, lipids, models, peptides, quartz crystal microbalance
- γ-zein peptides (VHLPPP)n present great potential as efficient molecule carriers across the cell membrane. To further understand the binding behavior of peptides with cell membrane, simplified models consisting of peptides and mono/bi-layer membranes (Langmuir monolayer and liposome) were used to studied the resulting response in the structure of peptide and cell membrane in the present work. The results showed that (VHLPPP)n=1,3 bound to dipalmitoylphosphatidylcholine (DPPC) liposomes and was induced to self-assemble into polyproline II (PP II) structure. The incorporation of (VHLPPP)n=1,3 in the DPPC Langmuir monolayers resulted in an increase in the surface pressure and a decrease in the collapse pressure, suggesting the increase of lipid monolayer fluidity. Fluorescence images further confirmed that the presence of (VHLPPP)n=1,3 promoted the formation of liquid-expanded (LE, dis-ordered) phases in lipid monolayers. Atomic force microscopy images found that (VHLPPP)n=1,3 preferred to penetrate in LE phase domains. In addition, (VHLPPP)3 possesses higher binding affinity with DPPC membrane models compared to (VHLPPP)1.