Formation of a Mimetic Biomembrane from the Hydrophobic Protein Zein and Phospholipids: Structure and Application

Abstract

α-Zein, a storage protein in corn endosperm, could be purified easily and in large amounts. In this study, α-zein was incorporated into phospholipid–cholesterol (PC–Chol) liposomes. The maximal amount of α-zein incorporated in the liposome was 0.05% (mol/mol) and the PC:Zein molar ratio was near 2400. At this level of zein insertion, the phase transition temperature of the lipid bilayer was little affected, but the leakage of doxorubicin (DOX) from the PC–Chol liposome became obviously slower when α-zein was added at a higher temperature than the phase transition temperature. Cryogenic transmission electron micrographs of the PC–Chol–Zein liposome showed that adjacent membranes in multilamellar vesicles were often aligned at a regular interval of about 7 nm. Data from synchrotron small-angle X-ray scattering of the PC–Chol–Zein liposome indicated the formation of the multilamellar structure with an intermembrane interval of 7.2 nm, whereas no homogeneous membrane alignment was observed in the absence of z...