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  • Title: Atomic force microscopy analysis of the Huntington protein nanofibril formation.
    Author: Dahlgren PR, Karymov MA, Bankston J, Holden T, Thumfort P, Ingram VM, Lyubchenko YL.
    Journal: Nanomedicine; 2005 Mar; 1(1):52-7. PubMed ID: 17292058.
    Abstract:
    BACKGROUND: Huntington's disease is an autosomal dominant progressive neurodegenerative disease associated with dramatic expansion of a polyglutamine sequence in exon 1 of the huntingtin protein htt that leads to cytoplasmic, and even nuclear aggregation of fibrils. METHODS: We have studied the in vitro fibril formation of mutant exon 1, and the shorter wild-type exon 1, with use of atomic force microscopy (AFM). RESULTS: Large aggregates are formed spontaneously after cleavage of the glutathione-S-transferase fusion protein of the mutant exon 1 protein. The AFM data showed that, unlike fibrils assembled by such proteins as amyloid beta-peptide and alpha-synuclein, htt forms fibrils with extensive branched morphologic features. Branching can be observed even at earlier stages of the htt self-assembly, but the effect is much more pronounced at late stages of aggregation. We also found that fusing of htt with green fluorescent protein does not change the branched-type morphologic features of the aggregates. CONCLUSIONS: On the basis of the results obtained, we propose a model for htt fibrillization that explains branched morphologic features of the aggregates.
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