| Literature DB >> 16602727 |
Natalya I Topilina1, Seiichiro Higashiya, Narender Rana, Vladimir V Ermolenkov, Christopher Kossow, Autumn Carlsen, Silvana C Ngo, Christopher C Wells, Eric T Eisenbraun, Kathleen A Dunn, Igor K Lednev, Robert E Geer, Alain E Kaloyeros, John T Welch.
Abstract
A de novo, genetically engineered 687 residue polypeptide expressed in E. coli has been found to form highly rectilinear, beta-sheet containing fibrillar structures. Tapping-mode atomic force microscopy, deep-UV Raman spectroscopy, and transmission electron microscopy definitively established the tendency of the fibrils to predominantly display an apparently planar bilayer or ribbon assemblage. The ordered self-assembly of designed, extremely repetitive, high molecular weight peptides is a harbinger of the utility of similar materials in nanoscience and engineering applications.Entities:
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Year: 2006 PMID: 16602727 DOI: 10.1021/bm0509016
Source DB: PubMed Journal: Biomacromolecules ISSN: 1525-7797 Impact factor: 6.988