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Søren Vrønning Hoffmann

Identification of a Novel Parallel beta-Strand Conformation within Molecular Monolayer of Amyloid Peptide

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The differentiation of protein properties and biological functions arises from the variation in the primary and secondary structure. Specifically, in abnormal assemblies of protein, such as amyloid peptide, the secondary structure is closely correlated with the stable ensemble and the cytotoxicity. In this work, the early A beta(33-42) aggregates forming the molecular monolayer at hydrophobic interface are investigated. The molecular monolayer of amyloid peptide A beta(33-42) consisting of novel parallel beta-strand-like structure is further revealed by means of a quantitative nanomechanical spectroscopy technique with force controlled in pico-Newton range, combining with molecular dynamic simulation. The identified parallel beta-strand-like structure of molecular monolayer is distinct from the antiparallel beta-strand structure of A beta(33-42) amyloid fibril. This finding enriches the molecular structures of amyloid peptide aggregation, which could be closely related to the pathogenesis of amyloid disease.

Original languageEnglish
Article number1500369
JournalAdvanced Science
Volume3
Issue6
Number of pages10
DOIs
Publication statusPublished - Jun 2016

    Research areas

  • ALZHEIMERS-DISEASE, FORCE MICROSCOPY, FIBRIL FORMATION, PROTEIN, OLIGOMERS, SPECTROSCOPY, MECHANISM, BEAMLINES, TOXICITY, MODEL

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