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Helical‐Ribbon Formation by a β‐Amino Acid Modified Amyloid β‐Peptide Fragment |
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| Authors: | Valeria Castelletto Dr. Ian W. Hamley Prof. Rohan A. Hule Dr. Darrin Pochan Prof. |
| Affiliation: | 1. Department of Chemistry, University of Reading, Whiteknights, Reading RG6 6AD (UK), Fax: (+44)?118‐378‐6341;2. Diamond Light Source, Didcot, Oxon OX11 0DE (UK);3. Department of Materials Science and Delaware Biotechnology Institute, Newark DE 19716 (USA);4. Current address: Department of Chemical Engineering, California Institute of Technology, 210‐41, Pasadena, CA 91125 (USA) |
| Abstract: | An addition to the family : The introduction of β‐amino acid residues into a modified amyloid β peptide fragment resulted in well‐defined helical nanoribbons (see cryo‐TEM image) comprising β strands mainly oriented perpendicular to the ribbon axis. The nanoribbons order into a flow‐aligning nematic phase at higher concentration. The β‐strand nanoribbon structure is an addition to the known set of secondary structures adopted by β‐peptides.  |
| Keywords: | β sheets amyloid β ‐peptides fibrils helical structures self‐assembly |