Exploring the interaction of the surfactant N-terminal domain of gamma-Zein with soybean phosphatidylcholine liposomes.
Zeins are maize storage proteins that accumulate inside large vesicles called protein bodies. gamma-Zein lines the inner surface of the protein body membrane, and its N-terminal, proline-rich, repetitive domain with the sequence (VHLPPP)(8) appears to be necessary for the accumulation of the protein within the organelle. Synthetic (VHLPPP)(8) adopts an amphipathic polyproline II conformation and forms cylindrical micelles in aqueous solution. Here we explore the interaction of (VHLPPP)(8) with soybean phosphatidylcholine unilamellar lipid vesicles and examine its effect on the stability and permeability of the liposome membrane. The amphipathic N-terminal domain of gamma-zein interacts with the membrane and assembles to form extended domains over the phospholipid membrane. The interaction between the peptide and the membrane increases the stability and permeability of the liposome membrane. The spontaneous amphipathic aggregation of (VHLPPP)(8) on the membrane suggests a mechanism of gamma-zein deposition inside maize protein bodies.
Kogan
Marcelo J
MJ
Institut de Recerca Biomédica de Barcelona, PCB, Josep Samitier 1, E-08028-Barcelona, Spain.
López
Olga
O
Cocera
Mercè
M
López-Iglesias
Carmen
C
De La Maza
Alfonso
A
Giralt
Ernest
E
D004721:Endoplasmic Reticulum / Q000378:metabolism; D005614:Freeze Fracturing; D008081:Liposomes / Q000737:chemistry* / Q000378:metabolism; D008854:Microscopy, Electron; D008958:Models, Molecular; D009842:Oligopeptides / Q000378:metabolism; D010539:Permeability; D010713:Phosphatidylcholines / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D013025:Glycine max / Q000737:chemistry*; D013501:Surface-Active Agents / Q000737:chemistry; D013997:Time Factors; D015028:Zein / Q000737:chemistry* / Q000378:metabolism
D008081:Liposomes; D009842:Oligopeptides; D010713:Phosphatidylcholines; D013501:Surface-Active Agents; D015028:Zein