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Issue 45, 2011
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The yin and yang of amyloid: insights from α-synuclein and repeat domain of Pmel17

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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.

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

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Publication details

The article was received on 29 Apr 2011, accepted on 15 Sep 2011 and first published on 12 Oct 2011


Article type: Perspective
DOI: 10.1039/C1CP21376H
Citation: Phys. Chem. Chem. Phys., 2011,13, 20066-20075
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    The yin and yang of amyloid: insights from α-synuclein and repeat domain of Pmel17

    R. P. McGlinchey, T. L. Yap and J. C. Lee, Phys. Chem. Chem. Phys., 2011, 13, 20066
    DOI: 10.1039/C1CP21376H

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