From Pathology to Materials Science and Engineering: Harnessing the Amyloid State for Biotechnological Applications

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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Publication Details

Journal
ACS Applied Materials & Interfaces
Published
2025-11-10
DOI
https://doi.org/10.1021/acsami.5c11847
Citations
2
Primary Topic
Supramolecular Self-Assembly in Materials
Type
article
Field-Weighted Citation Impact
1.19
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article

From Pathology to Materials Science and Engineering: Harnessing the Amyloid State for Biotechnological Applications

Enoch A. Nagelli, Chandramouli Natarajan, F. John Burpo, Ryan Limbocker et al.
2 citations
ACS Applied Materials & Interfaces
Supramolecular Self-Assembly in Materials
1.19
article

From Pathology to Materials Science and Engineering: Harnessing the Amyloid State for Biotechnological Applications

Enoch A. Nagelli, Chandramouli Natarajan, F. John Burpo, Ryan Limbocker, Lucas B. Fallot, Charles A. Anderson
article en
2 citations

Abstract

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.

ACS Applied Materials & InterfacesVol. 17(46)
United States Military Academy (US), Photonics (United States) (US), Department of Physics, Mathematics and Informatics (BY), American Military Academy (PR)
Openalex Percentile: Top 19%
Supramolecular Self-Assembly in Materials
1.19
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From Pathology to Materials Science and Engineering: Harnessing the Amyloid State for Biotechnological Applications — Enoch A. Nagelli, Chandramouli Natarajan, et al. · ACS Applied Materials & Interfaces (2025) | TGRS Research Map | TGRS