期刊
BIOCHEMICAL SOCIETY TRANSACTIONS
卷 33, 期 -, 页码 1106-1110出版社
PORTLAND PRESS LTD
DOI: 10.1042/BST0331106
关键词
amyloid; fibril; Parkinson's disease; beta-sheet-breaker peptide; alpha-synuclein
There is strong evidence for the involvement of a-synuclein in the pathologies of several neurodegenerative disorders, including PD (Parkinson's disease). Development of disease appears to be linked to processes that increase the rate at which alpha-synuclein forms aggregates. These processes include increased protein concentration (via either increased rate of synthesis or decreased rate of degradation), and altered forms of alpha-synuclein (such as truncations, missense mutations, or chemical modifications by oxidative reactions). Aggregated forms of the protein are toxic to cells and one therapeutic strategy would be to reduce the rate at which aggregation occurs. To this end we have designed several peptides that reduce alpha-synuclein aggregation. A cell-permeable version of one such peptide was able to inhibit the DNA damage induced by Fe(II) in neuronal cells transfected with alpha-synuclein (AS3T), a familial PD-associated mutation.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据