Amyloids are insoluble fibrous protein aggregates which are found in non-disease (functional) and disease states in a broad range of organisms including mammals. They have been the focus of intense research efforts world-wide because of occurrence in human diseases such as Parkinson’s, Alzheimer’s, Huntington’s and Diabetes mellitus (type II).
A paper describing the first atomic resolution study of an entire functional amyloid (in this case a fungal hydrophobin, EASΔ15) has been published in Angewandte Chemie, one of the world’s leading chemistry journals.
This was the result of collaboration between Karyn Wilde and Anthony Duff from the National Deuteration Facility and the University of Sydney (Sunde Lab). Multiple-labelled (2H/13C/15N) protein produced in the biodeuteration labs of the NDF was instrumental in enabling the solid-state NMR study of its structure.
Hydrophobins are fungal proteins that assemble into an amphipathic fibrillar monolayer with amyloid properties and a hydrophobic face as water-resistant as Teflon. Solid-state NMR studies on EAS hydrophobin fibrils reveal direct evidence of a partial molecular rearrangement on assembly and an ordered β-sheet-rich core in the context of a whole protein in this functional amyloid.
The title and full author list are as follows: “Solid-state NMR study of fungal hydrophobin rodlets, a functional amyloid, reveals a well-ordered β–sheet core amidst structural heterogeneity” by Vanessa Morris, Rasmus Linser, Karyn Wilde, Anthony Duff, Margaret Sunde and Ann Kwan.
Published: 05/11/2012