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

Content Provider	Semantic Scholar
Author	Al-Garawi, Zahraa S. Morris, Kyle L. Marshall, Karen E. Eichler, Jutta Serpell, Louise C.
Copyright Year	2017
Abstract	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.
File Format	PDF HTM / HTML
DOI	10.1098/rsfs.2017.0027
PubMed reference number	29147557
Journal	Medline
Volume Number	7
Alternate Webpage(s)	http://sro.sussex.ac.uk/id/eprint/71680/1/InterfaceFocus2017.pdf
Alternate Webpage(s)	http://rsfs.royalsocietypublishing.org/content/royfocus/7/6/20170027.full.pdf
Alternate Webpage(s)	http://sro.sussex.ac.uk/71680/1/InterfaceFocus2017.pdf
Journal	Interface Focus
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article