Research overview
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The aberrant misfolding and aggregation process of specific peptides and proteins plays a seminal role in the onset and development of over 60 protein misfolding diseases, including Alzheimer's and Parkinson's diseases. These proteins can convert from the endogenous, monomeric, and often largely intrinsically disordered state to the pathological, highly ordered amyloid state, which results in the formation of long, thread-like fibrillar species with extensive β-sheet structure and hallmark tinctorial and biophysical properties. Beyond pathology, the amyloid state has been well-studied for its role in physiological processes in numerous organisms through functional amyloids. In this review, we consider principles governing amyloid formation, with a focus on leveraging the unique biophysical properties and templating abilities of amyloids to produce diverse amyloid-containing materials with wide-ranging biotechnological applications, including, but not limited to, aerogels and hydrogels of varied function, drug delivery, tissue engineering, antimicrobials, purification and detection, protein-based packaging and food science, chemical catalysis, and bioelectronics. We conclude with a brief discussion on the opportunities and challenges ahead for implementing amyloid-based biotechnologies in society.
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