Antibodies against the C-terminus of α-synuclein modulate its fibrillation

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• 作者：Cagla Sahin^a ; ^b ; Nikolai Lorenzen^a ; ^b ; ^c ; Lasse Lemminger^a ; ^b ; Gunna Christiansen^d ; Ian Max Mø ; ller^e ; Louise Buur Vesterager^f ; Lars Ø ; stergaard Pedersen^f ; Karina Fog^f ; Pekka Kallunki^f ; Daniel E. Otzen^a ; ^b ; ^{dao@inano.au.dk}
• 关键词：Aβ ; amyloid-β ; aSN ; α-synuclein ; DOPG ; dioleoyl-phosphatidylglycerol ; EGCG ; Epigallocatechin gallate ; ELISA ; enzyme-linked immunosorbent assay ; LUV ; large unilamellar vesicles ; mAbs ; monoclonal antibodies ; NAC ; non-Amyloid beta component ; NC ; negative control ; PD ; Parkinson's disease ; RT ; room temperature ; ThT ; Thioflavin T
• 刊名：Biophysical Chemistry
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：220
• 期：Complete
• 页码：34-41
• 全文大小：1006 K
• 卷排序：220

文摘

Antibodies targeting the C-terminus of alpha synuclein inhibit its fibrillation. Antibody-bound oligomers show reduced permeabilization of lipid membranes. Increased avidity for oligomers and fibrils is ascribed to multiple epitopes.