ArticleThe Biochemical journal2013
Exploring the sequence-structure relationship for amyloid peptides.
Article in The Biochemical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Quantification of amyloid fibril polymorphism by nano-morphometry reveals the individuality of filament assembly.Communications chemistry · 2020Article
- Half a century of amyloids: past, present and future.Chemical Society reviews · 2020Review
- Solubility of proteins.ADMET & DMPK · 2020Article
- The Molecular Basis for Apolipoprotein E4 as the Major Risk Factor for Late-Onset Alzheimer's Disease.Journal of molecular biology · 2019Article
- The diversity and utility of amyloid fibrils formed by short amyloidogenic peptides.Interface focus · 2017Review
- Self-assembling peptide-based building blocks in medical applications.Advanced drug delivery reviews · 2017Review
- Dementia of the eye: the role of amyloid beta in retinal degeneration.Eye (London, England) · 2015Review
- Comparative modeling of hypothetical amyloid pores based on cylindrin.Journal of molecular modeling · 2015Article
- Fiber diffraction of the prion-forming domain HET-s(218-289) shows dehydration-induced deformation of a complex amyloid structure.Biochemistry · 2014Article
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Authors and funding
7 authors.
Funding
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.
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Registered trials
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