Bilayer Fibril Formation by Genetically Engineered Polypeptides:  Preparation and Characterization

• Published in: Biomacromolecules Vol. 7; no. 4; pp. 1104 - 1111
• Main Authors: Topilina, Natalya I, Higashiya, Seiichiro, Rana, Narender, Ermolenkov, Vladimir V, Kossow, Christopher, Carlsen, Autumn, Ngo, Silvana C, Wells, Christopher C, Eisenbraun, Eric T, Dunn, Kathleen A, Lednev, Igor K, Geer, Robert E, Kaloyeros, Alain E, Welch, John T
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 01-04-2006
• Subjects: Base Sequence; Biological and medical sciences; Biotechnology; DNA - chemistry; DNA - genetics; Fundamental and applied biological sciences. Psychology; Lipid Bilayers - chemical synthesis; Lipid Bilayers - chemistry; Lipid Bilayers - isolation & purification; Microscopy, Atomic Force; Microscopy, Electron, Transmission; Molecular Sequence Data; Molecular Weight; Particle Size; Peptides - chemical synthesis; Peptides - chemistry; Peptides - isolation & purification; Protein Conformation; Protein Engineering; Protein Structure, Secondary; Sensitivity and Specificity; Spectrum Analysis, Raman; Genetic engineering; Polypeptide; Application; Fibril
• ISSN: 1525-7797; 1526-4602
• DOI: 10.1021/bm0509016

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.