Inhibition of Huntingtin Exon-1 Aggregation by the Molecular Tweezer CLR01.
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ABSTRACT:
SUBMITTER: Vopel T
PROVIDER: S-EPMC5506490 | biostudies-literature | 2017 Apr
REPOSITORIES: biostudies-literature
Publications
Inhibition of Huntingtin Exon-1 Aggregation by the Molecular Tweezer CLR01.
Vöpel Tobias T Bravo-Rodriguez Kenny K Mittal Sumit S Vachharajani Shivang S Gnutt David D Sharma Abhishek A Steinhof Anne A Fatoba Oluwaseun O Ellrichmann Gisa G Nshanian Michael M Heid Christian C Loo Joseph A JA Klärner Frank-Gerrit FG Schrader Thomas T Bitan Gal G Wanker Erich E EE Ebbinghaus Simon S Sanchez-Garcia Elsa E
Journal of the American Chemical Society 20170413 16
Huntington's disease is a neurodegenerative disorder associated with the expansion of the polyglutamine tract in the exon-1 domain of the huntingtin protein (htt<sup>e1</sup>). Above a threshold of 37 glutamine residues, htt<sup>e1</sup> starts to aggregate in a nucleation-dependent manner. A 17-residue N-terminal fragment of htt<sup>e1</sup> (N17) has been suggested to play a crucial role in modulating the aggregation propensity and toxicity of htt<sup>e1</sup>. Here we identify N17 as a potent ...[more]
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