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The yin and yang of amyloid: insights from α-synuclein and repeat domain of Pmel17.

Authors
Type
Published Article
Journal
Physical Chemistry Chemical Physics
1463-9084
Publisher
The Royal Society of Chemistry
Publication Date
Volume
13
Issue
45
Pages
20066–20075
Identifiers
DOI: 10.1039/c1cp21376h
PMID: 21993592
Source
Medline

Abstract

Amyloid has been traditionally viewed in the context of disease. However, the emerging concept of 'functional amyloid' has taken a new direction into how we view amyloid. Recent studies have identified amyloid fibrils ranging from bacteria to humans that have a beneficial role, instead of being associated with a misfolded state that has been implicated in diseases such as Alzheimer's, Parkinson's and prion diseases. Here, we review our work on two human amyloidogenic polypeptides, one associated with Parkinson's disease, α-synuclein (α-syn), and the other important for melanin synthesis, the repeat domain (RPT) from Pmel17. Particularly, we focused our attention on spectroscopic studies of protein conformation and dynamics and their impact on α-syn amyloid formation and for RPT, we discussed the strict pH dependence of amyloid formation and its role in melanin biosynthesis.

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