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Functional amyloid--from bacteria to humans.

Douglas M Fowler¹, Atanas V Koulov, William E Balch

¹Department of Chemistry and The Skaggs Institute of Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

Trends in Biochemical Sciences

|April 7, 2007

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Amyloid proteins, once thought only harmful, are now known to have essential functions across many species. Understanding these functional amyloids offers new therapeutic strategies for amyloid-related diseases.

Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Amyloid proteins were historically associated with detrimental effects in human diseases.
Recent research reveals functional roles for amyloid structures in diverse organisms.

Purpose of the Study:

To explore the diverse physiological functions of amyloid structures.
To investigate the regulatory mechanisms of functional amyloidogenesis.
To re-evaluate the therapeutic potential of amyloid research.

Main Methods:

Literature review of recent studies on functional amyloids.
Analysis of specific examples like human Pmel17 and factor XII.
Comparative analysis of amyloid structures across different species.

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Main Results:

Identified functional amyloid fibers in bacteria, fungi, insects, invertebrates, and humans.
Highlighted roles in melanin biosynthesis (Pmel17) and hemostasis (factor XII).
Emphasized the necessity of tight regulation to prevent toxicity in functional amyloidogenesis.

Conclusions:

Functional amyloids represent a significant departure from their previously understood pathological roles.
Understanding the physiological applications of amyloid folds can inform new therapeutic approaches.
Further research into functional amyloidogenesis is crucial for treating amyloid diseases.