The diversity and utility of amyloid fibrils formed by short amyloidogenic peptides

Al-Garawi, Zahraa S, Morris, Kyle L, Marshall, Karen E, Eichler, Jutta and Serpell, Louise C (2017) The diversity and utility of amyloid fibrils formed by short amyloidogenic peptides. Interface Focus, 7 (6). p. 20170027. ISSN 2042-8898

[img] PDF - Published Version
Available under License Creative Commons Attribution.

Download (1MB)


Amyloidogenic peptides are well known for their involvement in diseases such as type 2 diabetes and Alzheimer's disease. However, more recently, amyloid fibrils have been shown to provide scaffolding and protection as functional materials in a range of organisms from bacteria to humans. These roles highlight the incredible tensile strength of the cross-β amyloid architecture. Many amino acid sequences are able to self-assemble to form amyloid with a cross-β core. Here we describe our recent advances in understanding how sequence contributes to amyloidogenicity and structure. For example, we describe penta- and hexapeptides that assemble to form different morphologies; a 12mer peptide that forms fibrous crystals; and an eight-residue peptide originating from α-synuclein that has the ability to form nanotubes. This work provides a wide range of peptides that may be exploited as fibrous bionanomaterials. These fibrils provide a scaffold upon which functional groups may be added, or templated assembly may be performed.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Research Centres and Groups: Dementia Research Group
Depositing User: Louise Serpell
Date Deposited: 30 Nov 2017 14:47
Last Modified: 30 Nov 2017 14:47

View download statistics for this item

📧 Request an update