Due to their natural abundance, functional diversity, and biocompatibility, proteins are an interesting class of biomolecule building-block for the fabrication of functional materials. In nature, proteins exist in a semi-stable “native” conformation; however, proteins can also self-assemble into organized aggregated conformations called amyloid fibers. Amyloid fibers have exceptional stability and material properties vastly different than the native proteins they are assembled from. Here, protein amyloid fibers will be introduced and discussed in the context of controlled functionality, and practical application, with an emphasis on understanding key structure-property relationships in the design of functional materials. In particular, the use of common proteins such as lysozyme and bovine serum albumin (BSA) and various synthetic pathways for the preparation of amyloid fibers are highlighted, describing their effects on kinetics of self-assembly, fiber morphology, and surface charge.<br/><br/>In addition, the interactions between amyloid fibers and nanocellulose are discussed, as relating to the preparation of composite materials. A particular emphasis is placed on the fabrication of composite films with chiral nematic structuring, assembled via evaporation-induced self-assembly. Here, we investigate the concentration-dependent incorporation of positively charged lysozyme amyloid fibers and negatively charged BSA amyloid fibers in relation to chiral nematic film structuring. We also demonstrate the effects of amyloid fiber incorporation on other physical properties including antibacterial activity and adhesiveness. Taken together, we anticipate that engineering the design of protein amyloid fibers and their interactions with nanocellulose will pave the way for a new generation of smart composite materials with enhanced functionalities.

Modulating interactions between protein amyloid fibers and nanocellulose towards advanced applications

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ACS Spring 2023

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