Evidence map›Paper›PMID 41211864›Full record

ReviewACS applied materials & interfaces2025

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

Lucas B Fallot, Chandramouli Natarajan, Carol A Anderson, Enoch A Nagelli, F John Burpo, Ryan Limbocker

Abstract readReview
In one paragraph

Review in ACS applied materials & interfaces, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Reverse-engineering amyloid strains with generative protein design.bioRxiv : the preprint server for biology · 2026
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Lucas B FallotDepartment of Chemical and Biological Science and Engineering, United States Military Academy, West Point, New York 10996, United States.ORCID 0000-0003-3056-2947
Chandramouli NatarajanDepartment of Chemical and Biological Science and Engineering, United States Military Academy, West Point, New York 10996, United States.
Carol A AndersonDepartment of Chemical and Biological Science and Engineering, United States Military Academy, West Point, New York 10996, United States.
Enoch A NagelliDepartment of Chemical and Biological Science and Engineering, United States Military Academy, West Point, New York 10996, United States.ORCID 0000-0003-2629-3174
F John BurpoDepartment of Chemical and Biological Science and Engineering, United States Military Academy, West Point, New York 10996, United States.ORCID 0000-0002-0303-1043
Ryan LimbockerDepartment of Chemical and Biological Science and Engineering, United States Military Academy, West Point, New York 10996, United States.ORCID 0000-0002-6030-6656

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

AmyloidBiotechnologyMaterials ScienceAnimalsHumansHydrogelsTissue EngineeringAmyloidHydrogelsantimicrobialsbioelectronicsbiophysicscatalysisdetectiondrug deliverypurificationtissue engineering

Identifiers

PMID41211864
PMCPMC12635977

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.