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Publication Abstract from PubMed

The hydrophobin EAS from the fungus Neurospora crassa forms functional amyloid fibrils called rodlets that facilitate spore formation and dispersal. Self-assembly of EAS into fibrillar rodlets occurs spontaneously at hydrophobic:hydrophilic interfaces and the rodlets further associate laterally to form amphipathic monolayers. We have used site-directed mutagenesis and peptide experiments to identify the region of EAS that drives intermolecular association and formation of the cross-beta rodlet structure. Transplanting this region into a nonamyloidogenic hydrophobin enables it to form rodlets. We have also determined the structure and dynamics of an EAS variant with reduced rodlet-forming ability. Taken together, these data allow us to pinpoint the conformational changes that take place when hydrophobins self-assemble at an interface and to propose a model for the amphipathic EAS rodlet structure.

Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS.,Macindoe I, Kwan AH, Ren Q, Morris VK, Yang W, Mackay JP, Sunde M Proc Natl Acad Sci U S A. 2012 Apr 3;109(14):E804-11. Epub 2012 Jan 23. PMID:22308366^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.