Self-assembled peptidic architecture with a tooth shape: folding into shape

Cited 63 time in scopus
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Title
Self-assembled peptidic architecture with a tooth shape: folding into shape
Author(s)
S Kwon; H S Shin; J Gong; J H Eom; A Jeon; S H Yoo; Im Sik Chung; S J Cho; H S Lee
Bibliographic Citation
Journal of American Chemical Society, vol. 133, no. 44, pp. 17618-17621
Publication Year
2011
Abstract
Molecular self-assembly is the spontaneous association of molecules into structured aggregates by which nature builds complex functional systems. While numerous examples have focused on 2D self-assembly to understand the underlying mechanism and mimic this process to create artificial nano- and microstructures, limited progress has been made toward 3D self-assembly on the molecular level. Here we show that a helical β-peptide foldamer, an artificial protein fragment, with well-defined secondary structure self-assembles to form an unprecedented 3D molecular architecture with a molar tooth shape in a controlled manner in aqueous solution. Powder X-ray diffraction analysis, combined with global optimization and Rietveld refinement, allowed us to propose its molecular arrangement. We found that four individual left-handed helical monomers constitute a right-handed superhelix in a unit cell of the assembly, similar to that found in the supercoiled structure of collagen.
ISSN
0002-7863
Publisher
Amer Chem Soc
DOI
http://dx.doi.org/10.1021/ja2082476
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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