Polymorphism of Amyloid Fibrils and their Complexes with Catalase

Nathaniel G.N. Milton, J. Robin Harris

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

2 Citations (Scopus)

Abstract

Catalase binding to amyloid fibrils has been shown for the Alzheimer's amyloid-β (Aβ), type 2 diabetes-associated islet amyloid polypeptide (IAPP) and Creutzfeldt-Jakob disease-associated prion protein (PrP). Catalase targets a specific domain with a GAII-like sequence and there are a number of other amyloid fibril-forming proteins that contain related sequences, such as the Parkinson's associated α-synuclein protein and the Huntington disease protein Huntingtin. Using transmission electron microscopy (TEM) analysis, interactions show specific binding of catalase to some, but not all, fibrillar forms of Aβ, IAPP and PrP fragments, allowing determination of the fibrillar forms that contain an accessible GAII-like sequence. The catalase-amyloid interactions have been used to identify novel amyloid-binding compounds such as the kisspeptins and oligo(ethylene glycol) derivatives of 6-methylbenzothiazole aniline. The use of TEM and other imaging techniques to study amyloid-catalase interactions has the potential for discovery of new therapeutics for amyloid-associated disorders.

Original languageEnglish
Title of host publicationBio-nanoimaging
Subtitle of host publicationProtein Misfolding and Aggregation
PublisherElsevier Inc.
Pages255-262
Number of pages8
ISBN (Print)9780123944313
DOIs
Publication statusPublished - Nov 2013
Externally publishedYes

Keywords

  • Amyloid fibrils
  • Catalase
  • Complexes
  • Polymorphism

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