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However, the molecular and structural basis underlying the increased toxicity of aggregates formed by proteins containing expanded polyQ repeats remain poorly understood, in part due to the size and morphological heterogeneity of the aggregates they form <jats:italic>in vitro<\/jats:italic>. To address this knowledge gap and technical limitations, we investigated the structural, mechanical and morphological properties of fibrillar aggregates at the single molecule and nanometer scale using the first exon of the Huntingtin protein as a model system (Exon1). Our findings demonstrate a direct correlation of the morphological and mechanical properties of Exon1 aggregates with their structural organization at the single aggregate and nanometric scale and provide novel insights into the molecular and structural basis of Huntingtin Exon1 aggregation and toxicity.<\/jats:p>","DOI":"10.1038\/srep31155","type":"journal-article","created":{"date-parts":[[2016,8,8]],"date-time":"2016-08-08T09:34:43Z","timestamp":1470648883000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":154,"title":["Nanoscale studies link amyloid maturity with polyglutamine diseases onset"],"prefix":"10.1038","volume":"6","author":[{"given":"F. 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