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    Effects of gamma-zein peptides on lipid membrane organization: Quartz crystal microbalance with dissipation and Langmuir monolayer studies

    Year: 2019

    Journal: Colloid Surf. A-Physicochem. Eng. Asp., Volume 574, AUG 5, page 86–93

    Authors: Zou, Yuan; Pan, Runting; Liu, Yingli; Liu, Xiao; Chen, Xiaowei; Wang, Jing; Wan, Zhili; Guo, Jian; Yang, Xiaoquan

    Organizations: Chinese National Natural Science FoundationNational Natural Science Foundation of China (NSFC) [31771923]; Guangdong Province Key Laboratory for Green Processing of Natural Products [KL-2018-01, KL-2018-09]; Open Project Program of China-Canada Joint Lab of Food Nutrition and Health, Beijing Technology and Business University (BTBU)

    Keywords: gamma-Zein peptide; Liposome; Langmuir monolayer; Interaction

    gamma-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).
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