Anika S Mostaert and Suzanne P Jarvis 2007 Nanotechnology 18 044010 doi:10.1088/0957-4484/18/4/044010
Anika S Mostaert and Suzanne P Jarvis
Show affiliationsWhile biological systems are notorious for their complexity, nature sometimes displays mechanisms that are elegant in their simplicity. We have recently identified such a mechanism at work to enhance the mechanical properties of certain natural adhesives. The mechanism is simple because it utilizes a non-specific protein folding and subsequent aggregation process, now thought to be generic for any polypeptide under appropriate conditions. This non-specific folding forms proteinaceous crossed β-sheet amyloid fibrils, which are usually associated with neurodegenerative diseases. Here we show evidence for the beneficial mechanical characteristics of these fibrils discovered in natural adhesives. We suggest that amyloid protein quaternary structures should be considered as a possible generic mechanism for mechanical strength in a range of natural adhesives and other natural materials due to their many beneficial mechanical features and apparent ease of self-assembly.
87.15.La Mechanical properties
87.85.Qr Nanotechnologies-design
Issue 4 (31 January 2007)
Received 14 August 2006, in final form 5 November 2006
Published 12 December 2006
Anika S Mostaert and Suzanne P Jarvis 2007 Nanotechnology 18 044010
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