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: Ryan P McGlinchey, Thai Leong Yap, Jennifer C Lee
• Journal: Physical chemistry chemical physics : PCCP (Phys Chem Chem Phys) Vol. 13 Issue 45 Pg. 20066-75 (Dec 07 2011) ISSN: 1463-9084 [Electronic] England
• PMID: 21993592 (Publication Type: Journal Article, Research Support, N.I.H., Intramural, Review)

Chemical References

• Amyloid
• Melanins
• PMEL protein, human
• alpha-Synuclein
• gp100 Melanoma Antigen

Topics

• Amyloid (chemistry, metabolism, ultrastructure)
• Humans
• Melanins (metabolism)
• Parkinson Disease (metabolism)
• Protein Conformation
• alpha-Synuclein (chemistry, metabolism)
• gp100 Melanoma Antigen (chemistry, metabolism)