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Reference: Vaux, David J., Jean, Létitia, Lee, Chiu Fan et al., Dynamics of the formation of a hydrogel by a pathogenic amyloid peptide: islet amyloid polypeptide. Scientific Reports, 6 (32124).Citable link to this page:

 

Dynamics of the formation of a hydrogel by a pathogenic amyloid peptide: islet amyloid polypeptide

Abstract: Many chronic degenerative diseases result from aggregation of misfolded polypeptides to formamyloids. Many amyloidogenic polypeptides are surfactants and their assembly can be catalysedby hydrophobic-hydrophilic interfaces (an air-water interface in-vitro or membranes in-vivo). Werecently demonstrated the specificity of surface-induced amyloidogenesis but the mechanisms ofamyloidogenesis and more specifically of adsorption at hydrophobic-hydrophilic interfaces remainpoorly understood. Thus, it is critical to determine how amyloidogenic polypeptides behave atinterfaces. Here we used surface tensiometry, rheology and electron microscopy to demonstratethe complex dynamics of gelation by full-length human islet amyloid polypeptide (involved in typeII diabetes) both in the bulk solution and at hydrophobic-hydrophilic interfaces (air-water interfaceand phospholipids). We show that the hydrogel consists of a 3D supramolecular network of fibrils. Wealso assessed the role of solvation and dissected the evolution over time of the assembly processes.Amyloid gelation could have important pathological consequences for membrane integrity and cellularfunctions.

Publication status:PublishedPeer Review status:Peer reviewedVersion:Publisher's versionDate of acceptance:02 August 2016Notes:© The Author(s) 2016. Published by Nature Publishing Group

Bibliographic Details

Publisher: Nature Publishing Group

Publisher Website: http://www.nature.com/index.html

Journal: Scientific Reportssee more from them

Publication Website: http://www.nature.com/srep/

Volume: 6

Issue: 32124Identifiers

Doi: https://doi.org/10.1038/srep32124

Issn: 2045-2322

Eissn: 2045-2322

Uuid: 6ed729f5-0ddc-480c-bf55-417bf4909e6e

Urn: uri:6ed729f5-0ddc-480c-bf55-417bf4909e6e

Pubs-id: pubs:637485 Item Description

Type: journal-article;

Version: Publisher's version

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Author: Vaux, David J. - Oxford, MSD, Pathology Dunn School Lincoln College - - - Jean, Létitia - Oxford, MSD, Pathology Dunn School fun

Source: https://ora.ox.ac.uk/objects/uuid:6ed729f5-0ddc-480c-bf55-417bf4909e6e



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