Conformational Targeting of Fibrillar Polyglutamine Proteins in Live Cells Escalates Aggregation and Cytotoxicity
作者： Erik Kvam , Brent L. Nannenga , Min S. Wang , Zongjian Jia , Michael R. Sierks
DOI: 10.1371/JOURNAL.PONE.0005727
关键词:
摘要: Background Misfolding- and aggregation-prone proteins underlying Parkinson's, Huntington's Machado-Joseph diseases, namely α-synuclein, huntingtin, ataxin-3 respectively, adopt numerous intracellular conformations during pathogenesis, including globular intermediates insoluble amyloid-like fibrils. Such conformational diversity has complicated research into amyloid-associated dysfunction neurodegeneration. To this end, recombinant single-chain Fv antibodies (scFvs) are compelling molecular tools that can be selected against specific protein conformations, expressed inside cells as intrabodies, for investigative therapeutic purposes.
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