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Exploring the sequence-structure relationship for amyloid peptides
journal contribution
posted on 2023-06-08, 14:28 authored by Kyle L Morris, Alison Rodger, Matthew R Hicks, Maya Debulpaep, Joost Schymkowitz, Frederic Rousseau, Louise SerpellLouise SerpellAmyloid 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
History
Publication status
- Published
Journal
Biochemical JournalISSN
0264-6021Publisher
Portland PressExternal DOI
Volume
450Page range
275-283Department affiliated with
- Biochemistry Publications
Full text available
- No
Peer reviewed?
- Yes
Legacy Posted Date
2013-02-14Usage metrics
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