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Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

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Polyphosphate: A Conserved Modifier of Amyloidogenic Processes.

Claudia M Cremers¹, Daniela Knoefler¹, Stephanie Gates²

¹Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.

|August 30, 2016

Summary

Polyphosphate (polyP) accelerates amyloid fibril formation in various proteins. This biopolymer also enhances bacterial biofilm formation and reduces amyloid toxicity in model organisms.

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Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Polyphosphate (polyP) is a ubiquitous biopolymer composed of inorganic phosphate chains.
PolyP is found in all studied cells, tissues, and organisms.
The functional roles of polyP in cellular processes are diverse and still being explored.

Purpose of the Study:

To investigate the potential role of polyP in amyloid fibril formation.
To determine if polyP influences the properties and in vivo effects of amyloid fibrils.

Main Methods:

In vitro assays to assess polyP's effect on amyloid nucleation and fibril formation for various proteins (CsgA, α-synuclein, Aβ1-40/42, Tau).
Characterization of polyP-associated amyloid fibrils (seeding, morphology, stability).
In vivo studies using bacterial biofilm formation models and C. elegans and neuroblastoma cell models for human folding diseases.

Main Results:

PolyP significantly accelerates amyloid fibril formation across a range of amyloidogenic proteins.
PolyP acts as an effective nucleation source for amyloid proteins.
PolyP-modified amyloid fibrils exhibit altered seeding, morphology, and stability.
In vivo, polyP increases bacterial biofilm formation and mitigates amyloid toxicity in cellular and organismal models.

Conclusions:

Polyphosphate is a potent accelerator of amyloid formation and a modifier of amyloid fibril properties.
PolyP demonstrates conserved cytoprotective effects against amyloidogenic processes in vivo.
These findings reveal a novel role for polyP as a regulator of protein aggregation and cellular stress response.