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Article ? AI-assigned paper type based on the abstract. Classification may not be perfect — flag errors using the feedback button. Tier 2 ? Original research — experimental, observational, or case-control study. Direct primary evidence. Human Health Effects Sign in to save

Amyloid Fibrils and Their Applications: Current Status and Latest Developments

Nanomaterials 2025 10 citations ? Citation count from OpenAlex, updated daily. May differ slightly from the publisher's own count. Score: 68 ? 0–100 AI score estimating relevance to the microplastics field. Papers below 30 are filtered from public browse.
Bingxu Liu, Hongnan Zhang, Xiaohong Qin

Summary

This review covers how certain proteins can naturally form tiny fiber-like structures called amyloid fibrils, which were first discovered in the brains of patients with neurodegenerative diseases. While primarily about bionanomaterials, the research is relevant to microplastics because nanoplastics have been shown to interact with proteins and potentially accelerate harmful amyloid formation in the body.

Body Systems
Models

Amyloid fibrils are one of the important forms of protein aggregates, first discovered in the pathological brain tissues of patients with various neurodegenerative diseases. They are considered the core pathological markers of different neurodegenerative diseases. In recent years, research has found that multiple proteins or peptides dynamically assemble to form functional amyloid-like nanofibrils under physiological conditions, exhibiting excellent mechanical properties, high environmental stability, and self-healing ability. Therefore, they have become a class of functional biological nanomaterials with important development potential. This article systematically reviews the latest progress in the preparation, functionalization, and application of amyloid-like nanofibrils in engineering and provides an outlook on possible future development directions.

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