Molecular Self-Assembly of Surfactant-like Peptides to Form Nanotubes and Nanovesicles

Several surfactant-like peptides undergo self-assembly to form nanotubes and nanovesicles having an average diameter of 30-50 nm with a helical twist. The peptide monomer contains 7-8 residues and has a hydrophilic head composed of aspartic acid and a tail of hydrophobic amino acids such as alanine,...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2002-04, Vol.99 (8), p.5355-5360
Main Authors: Vauthey, Sylvain, Santoso, Steve, Gong, Haiyan, Watson, Nicki, Zhang, Shuguang
Format: Article
Language:English
Subjects:
Alanine - chemistry
Amino acids
Aspartic Acid - chemistry
Biological Sciences
Biophysics - methods
Design
Leucine - chemistry
Light
Lipid Bilayers - chemistry
Lipids
Materials
Microscopy, Electron
Models, Molecular
Molecules
Nanostructures
Nanotechnology
Nanotubes
Peptides
Peptides - chemistry
Phospholipids - chemistry
Protein Conformation
Protein Folding
Protein Structure, Tertiary
Scaffolds
Scattering, Radiation
Self assembly
Surface-Active Agents - chemistry
Surfactants
Valine - chemistry
Water - chemistry
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Summary:Several surfactant-like peptides undergo self-assembly to form nanotubes and nanovesicles having an average diameter of 30-50 nm with a helical twist. The peptide monomer contains 7-8 residues and has a hydrophilic head composed of aspartic acid and a tail of hydrophobic amino acids such as alanine, valine, or leucine. The length of each peptide is ≈2 nm, similar to that of biological phospholipids. Dynamic light-scattering studies showed structures with very discrete sizes. The distribution becomes broader over time, indicating a very dynamic process of assembly and disassembly. Visualization with transmission electron microscopy of quick-freeze/deep-etch sample preparation revealed a network of open-ended nanotubes and some vesicles, with the latter being able to "fuse" and "bud" out of the former. The structures showed some tail sequence preference. Many three-way junctions that may act as links between the nanotubes have been observed also. Studies of peptide surfactant molecules have significant implications in the design of nonlipid biological surfactants and the understanding of the complexity and dynamics of the self-assembly processes.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.072089599