Exploring the sequence-structure relationship for amyloid peptides

Morris, Kyle L, Rodger, Alison, Hicks, Matthew R, Debulpaep, Maya, Schymkowitz, Joost, Rousseau, Frederic and Serpell, Louise C (2012) Exploring the sequence-structure relationship for amyloid peptides. Biochemical Journal, 450. pp. 275-283. ISSN 0264-6021

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Amyloid fibril formation is associated with misfolding diseases, as well as fulfilling a functional role. The cross-ß molecular architecture has been reported in increasing numbers of amyloid-like fibrillar systems. The Waltz algorithm is able to predict ordered self-assembly of amyloidogenic peptides by taking into account residue type and position. This algorithm has expanded the amyloid sequence space and here we characterise the structures of amyloid-like fibrils formed by three peptides identified by Waltz that form fibrils but not crystals. The structural challenge is met by combining electron microscopy, linear and circular dichroism and X-ray fibre diffraction. We propose structures that reveal a cross-ß conformation with 'steric-zipper' features, giving insights into the role for side chains in peptide packing and stability within fibrils. The amenity of these peptides to structural characterisation makes them compelling model systems to use for understanding the relationship between sequence, self-assembly, stability and structure for amyloid fibrils

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Subjects: Q Science > QD Chemistry > QD0241 Organic chemistry > QD0415 Biochemistry
Depositing User: Louise Serpell
Date Deposited: 14 Feb 2013 12:22
Last Modified: 21 May 2013 10:23
URI: http://sro.sussex.ac.uk/id/eprint/43764
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