Functional Amyloids

Dear Colleagues,

There is a growing recognition that the cross β amyloid architecture is found widely in nature, formed by the self-assembly of different proteins and associated with multiple and diverse aspects of normal biology in organisms from microbes to mammals. In so-called “functional amyloid” the amyloidogenic proteins provide desirable self-assembly capability and the biologically active form of the protein is retained or generated in the fibrillar form. The amyloid, multimeric version of the protein has properties beyond that of the monomeric component protein. Functional amyloid fibrils have been shown to have roles in bacterial biofilm formation, fungal adhesion and colonisation, melanin sequestration and subcellular localisation of proteins associated with gene regulation. Studies of disease-associated amyloid formation and structure have laid the foundations for investigation of functional amyloids but recent work on the latter is bringing to light some of the differences in the properties of biologically active and pathological amyloids. We hope that this special issue will highlight exciting recent work in this area as well as stimulate new avenues of research into the biological functions of amyloid, the regulation of functional amyloid and the potential application of amyloids as nanomaterials.

Followed by brief mention of different contributions, putting them in context with each other and the overall theme.

A/Prof. Dr. Margaret Sunde
A/Prof. Dr. Matthew Chapman
Prof. Dr. Daniel Otzen
Prof. Dr. Sarah Perrett
Guest Editors

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