title: The yin and yang of amyloid: insights from α-synuclein and repeat domain of Pmel17.
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.
authors: Laboratory of Molecular Biophysics, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland, USA.
authors: Ryan P
authors: RP
authors: McGlinchey
authors: Thai Leong
authors: TL
authors: Yap
authors: Jennifer C
authors: JC
authors: Lee
mesh_terms: D000682:Amyloid / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D008543:Melanins / Q000378:metabolism*; D010300:Parkinson Disease / Q000378:metabolism; D011487:Protein Conformation; D051844:alpha-Synuclein / Q000737:chemistry / Q000378:metabolism*; D058951:gp100 Melanoma Antigen / Q000737:chemistry / Q000378:metabolism*
chemical_list: D000682:Amyloid; D008543:Melanins; C548637:PMEL protein, human; D051844:alpha-Synuclein; D058951:gp100 Melanoma Antigen