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Nat Mater. 2010 May;9(5):454-60. doi: 10.1038/nmat2742. Epub 2010 Apr 11.

Free-floating ultrathin two-dimensional crystals from sequence-specific peptoid polymers.

Author information

1
Molecular Foundry; National Center for Electron Microscopy, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.

Abstract

The design and synthesis of protein-like polymers is a fundamental challenge in materials science. A biomimetic approach is to explore the impact of monomer sequence on non-natural polymer structure and function. We present the aqueous self-assembly of two peptoid polymers into extremely thin two-dimensional (2D) crystalline sheets directed by periodic amphiphilicity, electrostatic recognition and aromatic interactions. Peptoids are sequence-specific, oligo-N-substituted glycine polymers designed to mimic the structure and functionality of proteins. Mixing a 1:1 ratio of two oppositely charged peptoid 36mers of a specific sequence in aqueous solution results in the formation of giant, free-floating sheets with only 2.7 nm thickness. Direct visualization of aligned individual peptoid chains in the sheet structure was achieved using aberration-corrected transmission electron microscopy. Specific binding of a protein to ligand-functionalized sheets was also demonstrated. The synthetic flexibility and biocompatibility of peptoids provide a flexible and robust platform for integrating functionality into defined 2D nanostructures.

PMID:
20383129
DOI:
10.1038/nmat2742
[Indexed for MEDLINE]

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