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Functional Amyloids as Multifunctional Platforms for Targeted Drug Delivery and Immunotherapy.

Brianna McVay^1,2, Dana Wolfe^1,2, Ayyalusamy Ramamoorthy^1,2,3

¹Department of Chemical and Biomedical Engineering, FAMU-FSU College of Engineering, Florida State University, 2525 Pottsdamer Street, Tallahassee, Florida 32310, United States.

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|September 17, 2025

Summary

Amyloid fibrils, derived from self-assembling peptides, show promise as stable biomaterials for drug delivery and immunotherapy. Engineered amyloid nanostructures offer targeted delivery and enhanced immune responses, advancing precision medicine.

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Area of Science:

Biomaterials Science
Nanotechnology
Immunology

Background:

Self-assembling molecules are key to novel material design.
Amyloid fibrils, known from neurodegenerative diseases, are stable, biocompatible nanostructures.
Their potential in therapeutics and immunomodulation is increasingly recognized.

Purpose of the Study:

To review the design and application of functional amyloid nanostructures.
To highlight their role in targeted drug delivery and immunotherapy.
To discuss advancements in engineered amyloid-based platforms.

Main Methods:

Review of recent studies on amyloid fibril self-assembly and functionalization.
Analysis of amyloid fibrils' properties for encapsulation and targeting.
Examination of hybrid systems combining amyloid with liposomes and hydrogels.

Main Results:

Amyloid fibrils can encapsulate small molecules and be surface-functionalized for targeted delivery.
They enable environmentally responsive drug release and show potential in vaccine development.
Amyloid scaffolds act as carriers and adjuvants, enhancing immune activation.

Conclusions:

Engineered amyloid nanostructures offer versatile platforms for targeted drug delivery and immunotherapy.
Hybridization with existing delivery tools can improve therapeutic efficacy and reduce toxicity.
Further understanding of these platforms may drive precision medicine and innovative biomaterial design.