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Issue 10, 2010
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Fibres, crystals and polymorphism: the structural promiscuity of amyloidogenic peptides

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Abstract

The ability to assemble to form β-sheet rich fibrils in vitro is shared by a broad range of precursor proteins and peptides. The ordered aggregation and deposition of a number of specific polypeptides are associated with diseases including Alzheimer's disease and Diabetes type 2 and recently it has been shown that the highly stable nature of amyloid fibrils has been exploited by organisms as functional materials. Here we describe the capacity of peptides to form various different β-sheet rich structures, each sharing the amyloid-like structure, but differing in specific arrangements and side-chain interactions.

Graphical abstract: Fibres, crystals and polymorphism: the structural promiscuity of amyloidogenic peptides

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Publication details

The article was received on 17 Dec 2009, accepted on 03 Feb 2010 and first published on 22 Feb 2010


Article type: Highlight
DOI: 10.1039/B926623B
Citation: Soft Matter, 2010,6, 2110-2114
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    Fibres, crystals and polymorphism: the structural promiscuity of amyloidogenic peptides

    K. E. Marshall and L. C. Serpell, Soft Matter, 2010, 6, 2110
    DOI: 10.1039/B926623B

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