Bilayer Fibril Formation by Genetically Engineered Polypeptides: Preparation and Characterization
Biomacromolecules2006Vol. 7(4), pp. 1104–1111
Citations Over TimeTop 10% of 2006 papers
Natalya I. Topilina, Seiichiro Higashiya, Narender Rana, Vladimir V. Ermolenkov, Christopher Kossow, Autumn Carlsen, S.C. Ngo, Christopher C. Wells, Eric Eisenbraun, Kathleen Dunn, Igor K. Lednev, Robert 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, β-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.
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