The self-assembly of surfactant-like peptides containing 4-10 glycines as the component of the hydrophobic tails and aspartic acids as the hydrophilic heads is described. The peptide monomers form nanotubes and nanovesicles in water at neutral pH. These nanostructures become more polydisperse as the length of the glycine tails increases. These unique structures may serve not only as scaffolds for constructing diverse nanodevices but also as enclosures to encapsulate rudimentary enzymes for studying prebiotic molecular evolution.
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