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Functional Amyloids as Multifunctional Platforms for Targeted Drug Delivery and Immunotherapy
Brianna McVay1,2, Dana Wolfe1,2, Ayyalusamy Ramamoorthy1,2,3
1Department of Chemical and Biomedical Engineering, FAMU-FSU College of Engineering, Florida State University, 2525 Pottsdamer Street, Tallahassee, Florida 32310, United States.
None:
Self-assembly of molecules is increasingly utilized in the design and development of novel materials for various chemical and biomedical applications. Amyloid fibrils, traditionally associated with neurodegenerative diseases, make up a class of biomaterials formed through the self-assembly of peptides and proteins. The excellent stability and biocompatibility of cross-β-sheet nanostructured amyloid fibrils make them promising biomaterials for therapeutic delivery and immunomodulation. Recent studies have demonstrated the ability of amyloid fibrils to encapsulate small molecules, support receptor-specific targeting through surface functionalization, and enable environmentally responsive drug release. Amyloid-based scaffolds have also shown notable potential in vaccine development and the controlled delivery of checkpoint inhibitors. Current research aims to hybridize amyloid-based scaffolds with commonly used drug delivery tools, such as liposomes and hydrogels, to further enhance therapeutic efficacy while minimizing toxicity. In immunological applications, amyloid fibrils serve as both carriers and adjuvants, promoting antigen presentation and sustained immune activation. This review provides an overview of current progress in the design and application of functional amyloid nanostructures for targeted drug delivery and immunotherapy. The growing understanding of engineered amyloid-based drug delivery platforms may drive the development of precision medicine and support the design of innovative biomaterials.
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