Analysis of sheep α-synuclein provides a molecular strategy for the reduction of fibrillation

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• 作者：Lungisa Bickle ; ^{lungisa.bickle@sahmri.com} ; John J. Hopwood ; Litsa Karageorgos
• 关键词：α-Synuclein ; Parkinson's disease ; Amyloid ; Aggregation ; Fibril
• 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：1865
• 期：3
• 页码：261-273
• 全文大小：2609 K
• 卷排序：1865

文摘

Sheep α-synuclein formed fibrils less readily than human α-synuclein. Altering residues G68 and V95 in human α-synuclein reduced aggregation. “Sheep-like” human α-synuclein had markedly lower fibrillation than wild-type. “Human-like” sheep α-synuclein aggregated faster than the wild-type form.