Toward a soluble model system for the amyloid state

Nicole C. Thomas, Gail J. Bartlett, Derek N. Woolfson, Samuel H. Gellman*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

4 Citations (Scopus)
270 Downloads (Pure)


The formation and deposition of amyloids is associated with many diseases. β-Sheet secondary structure is a common feature of amyloids, but the packing of sheets against one another is distinctive relative to soluble proteins. Standard methods that rely on perturbing a polypeptide's sequence and evaluating impact on folding can be problematic for amyloid aggregates because a single sequence can adopt multiple conformations and diverse packing arrangements. We describe initial steps toward a minimum-sized, soluble model system for the amyloid state that supports comparisons among sequence variants. Critical to this goal is development of a new linking strategy to enable intersheet association mediated by side chain interactions, which is characteristic of the amyloid state. The linker design we identified should ultimately support exploration of relationships between sequence and amyloid state stability for specific strand-association modes.

Original languageEnglish
Pages (from-to)16434-16437
Number of pages4
JournalJournal of the American Chemical Society
Issue number46
Publication statusPublished - 8 Nov 2017

Structured keywords

  • BrisSynBio
  • Bristol BioDesign Institute


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