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• W2071640383 abstract "Abstract Neurodegenerative diseases are often associated with the formation of highly insoluble aggregates. Despite the efforts devoted to the characterization of these aggregates, their structure remains elusive. Several neurodegenerative diseases are characterized by the expansion of CAG repeats, which code for Gln. Among the structural models proposed for the aggregates observed in polyQ‐linked diseases, the nanotube β‐helix model proposed by Perutz and colleagues Proc Natl Acad Sci U S A 2002;99:5591–5595 has been influential. In the present study, the stability of this β‐helix model has been investigated by performing molecular dynamics simulations on polyQ fragments of different lengths. The results indicate that models shorter than two full β‐helix turns are unstable and collapse toward irregular structures. On the other hand, longer β‐helix models, containing more than 40 residues, achieve a dynamic regular structure. This finding is in line with the observed threshold of Gln repeats (≈ 40) correlated with the insurgence of the disease. Notably, the structure of the final state of the models longer than 40 residues strictly depends on their size. A compact stable ellipsoidal structure is formed by the model made of two full helical turns (41 residues), whereas water filled tubular structures emerge from simulation on longer polypeptides. These results have been interpreted taking into account the experimental data on polyQ aggregates. A structural interpretation of the literature data has been proposed by assuming that different β‐helical models are involved in the different stages of the aggregation process. Proteins 2006. © 2006 Wiley‐Liss, Inc." @default.
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• W2071640383 date "2006-03-02" @default.
• W2071640383 modified "2023-10-16" @default.
• W2071640383 title "Polyglutamine repeats and β-helix structure: Molecular dynamics study" @default.
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• W2071640383 doi "https://doi.org/10.1002/prot.20941" @default.
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