Structure, assembly, and biological activity of amyloid peptides and proteins.

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Amyloid fibrils are highly ordered filamentous structures formed by a wide range of different proteins and peptides. These assemblies were originally described as potential mediators of cytotoxicity in amyloidosis, and are linked to infectivity in prion diseases. More recently, amyloids been shown to play important functional roles in diverse biological processes ranging from assembly of the skin pigment melanin, genetic diversification of fungi and yeast and adhesion of bacteria and yeast to surfaces during biofilm formation. Despite their biological importance, the ability of diverse proteins to self-assemble into closely related structures having highly divergent function remains poorly understood. Similarly, it is not known how some of these assemblies can be potently cytotoxic while others avoid toxicity to perform biological tasks. This chemical and functional diversity, built on an ordered scaffold, is also a desirable feature in the development of novel biomaterials. Understanding the roles of amyloid proteins in biology, and exploiting their materials potential, both require detailed knowledge of the molecular basis for fibril formation, and the ability to link sequence with the structure and function of the fibrillar state.