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Exploring the sequence–structure relationship for amyloid peptides
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Morris, Kyle L., Rodger, Alison, Hicks, Matthew R., Debulpaep, Maya, Schymkowitz, Joost, Rousseau, F. (Frederic) and Serpell, Louise C. (2013) Exploring the sequence–structure relationship for amyloid peptides. Biochemical Journal, Vol.450 (No.2). pp. 275-283. doi:10.1042/BJ20121773 ISSN 0264-6021.
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Official URL: http://dx.doi.org/10.1042/BJ20121773
Abstract
Amyloid fibril formation is associated with misfolding diseases, as well as fulfilling a functional role. The cross-β 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 the residue type and position. This algorithm has expanded the amyloid sequence space, and in the present study we characterize 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 dichroism, CD and X-ray fibre diffraction. We propose structures that reveal a cross-β 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 characterization makes them compelling model systems to use for understanding the relationship between sequence, self-assembly, stability and structure of amyloid fibrils.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QD Chemistry Q Science > QP Physiology |
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry Faculty of Science, Engineering and Medicine > Research Centres > Molecular Organisation and Assembly in Cells (MOAC) |
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Library of Congress Subject Headings (LCSH): | Amyloid -- Structure, Algorithms, X-rays -- Diffraction, Amino acid sequence | ||||
Journal or Publication Title: | Biochemical Journal | ||||
Publisher: | Portland Press | ||||
ISSN: | 0264-6021 | ||||
Official Date: | 2013 | ||||
Dates: |
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Volume: | Vol.450 | ||||
Number: | No.2 | ||||
Page Range: | pp. 275-283 | ||||
DOI: | 10.1042/BJ20121773 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Open Access (Creative Commons) | ||||
Date of first compliant deposit: | 24 December 2015 | ||||
Date of first compliant Open Access: | 24 December 2015 | ||||
Funder: | Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Alzheimer’s Research UK |
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