While amyloid fibrils are usually associated with pathological aggregates of proteins and peptides in amyloid diseases, accumulating discoveries start to uncover functional roles of amyloids beyond pathology, known as functional amyloids. For example, amyloid fibrils formed by PMEL17 are a major functional component of the melanosomal compartment as they optimize melanin polymerization, condensation and storage. Beta-endorphin, an endogenous opioid peptide, forms amyloid fibrils in the low pH environment of secretory vesicles for efficient storage. Bacteria secret peptides (e.g., Curli CsgA in E. Coli, FapC in pseudomonas, and PSM in staphylococcus) to form amyloid fibrils important for biofilm formation. Vicilin amyloid accumulation increases during seed maturation and wanes at germination. In addition, amyloid fibrils have been discovered as building blocks for bionanotechnology and used to develop hybrid composite nanomaterials for novel applications. Recently, our lab starts to investigate structures and assembly dynamics of functional amyloids and explore their applications and implications.
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– Featured as the Cover.
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– Featured as the Cover.
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