Accessibility navigation


Self-assembly in aqueous solution of a modified amyloid beta peptide fragment

Castelletto, V., Hamley, I.W. and Harris, P.J.F. (2008) Self-assembly in aqueous solution of a modified amyloid beta peptide fragment. Biophysical Chemistry, 138 (1-2). pp. 29-35. ISSN 0301-4622

Full text not archived in this repository.

It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing.

To link to this item DOI: 10.1016/j.bpc.2008.08.007

Abstract/Summary

The self-assembly in films dried from aqueous solutions of a modified amyloid beta peptide fragment is studied. We focus on sequence A beta(16-20), KLVFF, extended by two alanines at the N-terminus to give AAKLVFF. Self-assembly into twisted ribbon fibrils is observed, as confirmed by transmission electron microscopy (TEM). Dynamic light scattering reveals the semi-flexible nature of the AAKLVFF fibrils, while polarized optical microscopy shows that the peptide fibrils crystallize after an aqueous solution of AAKLVFF is matured over 5 days. The secondary structure of the fibrils is studied by FT-IR, circular dichroism and X-ray diffraction (XRD), which provide evidence for beta-sheet structure in the fibril. From high resolution TEM it is concluded that the average width of an AAKLVFF fibril is (63 +/- 18) nm, indicating that these fibrils comprise beta-sheets with multiple repeats of the unit cell, determined by XRD to have b and c dimensions 1.9 and 4.4 nm with an a axis 0.96 nm, corresponding to twice the peptide backbone spacing in the antiparallel beta-sheet. (C) 2008 Elsevier B.V. All rights reserved.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences
Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
Interdisciplinary centres and themes > Chemical Analysis Facility (CAF)
ID Code:11097
Uncontrolled Keywords:Amyloid, Peptide, Fibrils, Self-assembly , DYNAMIC SCATTERING, SPECTROSCOPY, POLYPEPTIDES, POLYMERS, FIBRILS, SOLVENT
Publisher:Elsevier

University Staff: Request a correction | Centaur Editors: Update this record

Page navigation