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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 Serpell
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

History

Publication status

  • Published

Journal

Biochemical Journal

ISSN

0264-6021

Publisher

Portland Press

Volume

450

Page range

275-283

Department affiliated with

  • Biochemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2013-02-14

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    University of Sussex (Publications)

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