Dynamic structural determinants underlie the neurotoxicity of the N-terminal tau 26-44 peptide in Alzheimer's disease and other human tauopathies.

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ID: 29894
2019
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Ranked #161 of 200 articles by views in International journal of biological macromolecules

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Abstract
The intrinsically disordered tau protein plays a pivotal role in the pathogenesis of Alzheimer's disease (AD) and other human tauopathies. Abnormal post-translational modifications of tau, such as truncation, are causally involved in the onset/development of these neurodegenerative diseases. In this context, the AD-relevant N-terminal fragment mapping between 26 and 44 amino acids of protein (tau26-44) is interesting, being endowed with potent neurotoxic effects in vitro and in vivo. However, the understanding of the mechanism(s) of tau26-44 toxicity is a challenging task because, similarly to the full-length tau, it does not have a unique 3D structure but exists as dynamic ensemble of conformations. Here we use Atomic Force Spectroscopy, Small Angle X-ray Scattering and Molecular Dynamics simulation to gather structural and functional information on the tau26-44. We highlight the presence, the type and the location of its temporary secondary structures and we unveil the occurrence of relevant transient tertiary conformations that could contribute to tau26-44 toxicity. Data are compared with those obtained on the biologically-inactive, reverse-sequence (tau44-26 peptide) which has the same mass, charge, aminoacidic composition as well as the same overall unfolded character of tau26-44.
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perini2019dynamicinternational Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Perini, Giordano;Ciasca, Gabriele;Minelli, Eleonora;Papi, Massimiliano;Palmieri, Valentina;Maulucci, Giuseppe;Nardini, Matteo;Latina, Valentina;Corsetti, Veronica;Florenzano, Fulvio;Calissano, Pietro;De Spirito, Marco;Amadoro, Giuseppina;
Journal International journal of biological macromolecules
Year 2019
DOI
S0141-8130(19)33861-9
URL
Keywords Keywords not found

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