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Spontaneous Formation of Gating Lipid Domain in Uniform-Size Peptide Vesicles for Controlled Release
- Rahman, Md. Mofizur, Ueda, Motoki, Hirose, Takuji, Ito, Yoshihiro
- Journal of the American Chemical Society 2018 v.140 no.51 pp. 17956-17961
- biomimetics, drugs, energy transfer, fluorescein, fluorescence, hydrophilicity, mixing, models, permeability, phase transition, phospholipids, polyethylene glycol, polypeptides, temperature
- Hybrid assemblies composed of phospholipids and amphiphilic polymers have been investigated previously as a biomimetic model of biological cells. However, these studies focused on the functions of polymers in a sea of membrane lipids. Here, we prepared a highly stable peptide-lipid hybrid vesicle from a combination of an amphiphilic polypeptide and the phospholipid, 1,2-dimyristoyl-sn-glycero-3-phosphocholine, with a mixing molar ratio of 1:1. The phase-separated structure of the hybrid vesicle was demonstrated by fluorescence resonance energy transfer analysis. The lipid domain of the hybrid vesicle had a phase-transition temperature of 38 °C and allowed the permeation of a hydrophilic molecule, fluorescein isothiocyanate-labeled polyethylene glycol (Mw: 2000), above 38 °C. The designed peptide-lipid hybrid vesicle and a “lipidic gate” are a promising tool for smart drug delivery.