Amyloids are highly ordered, self-assembled protein aggregates most commonly associated with neurological diseases such as Alzheimer’s and Parkinson’s. However, their ability to self-assemble into highly stable aggregates or fibrils has been shown to enhance cellular functions such as cell growth, bio-adhesion, and mechanical strength in various organisms. The structural variety and robust mechanical properties of amyloid proteins make them attractive for biomaterial synthesis. The self-assembly of synthetic amyloid proteins was investigated under varying environmental conditions, and the morphology and nano-mechanical properties were characterized using atomic force microscopy (AFM) in quantitative nanomechanical mapping (QNM) mode. Protein self-assembly kinetics and adhesive properties were probed using quartz crystal microbalance with dissipation monitoring (QCM-D).

Nanomechanical and self-assembly properties of de novo amyloid peptides

ACS Spring 2022

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