Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/85006
Title: Identification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid Peptide
Authors: Liu, Lei
Li, Qiang
Zhang, Shuai
Wang, Xiaofeng
Hoffmann, Søren Vrønning
Li, Jingyuan
Liu, Zheng
Besenbacher, Flemming
Dong, Mingdong
Keywords: Atomic force microscopy
Amyloid peptide aggregation
Issue Date: 2016
Source: Liu, L., Li, Q., Zhang, S., Wang, X., Hoffmann, S. V., Li, J., et al. (2016). Identification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid Peptide. Advanced Science, 3(6), 1500369-.
Series/Report no.: Advanced Science
Abstract: 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 Aβ33-42 aggregates forming the molecular monolayer at hydrophobic interface are investigated. The molecular monolayer of amyloid peptide Aβ33-42 consisting of novel parallel β-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 β-strand-like structure of molecular monolayer is distinct from the antiparallel β-strand structure of Aβ33-42 amyloid fibril. This finding enriches the molecular structures of amyloid peptide aggregation, which could be closely related to the pathogenesis of amyloid disease.
URI: https://hdl.handle.net/10356/85006
http://hdl.handle.net/10220/42054
DOI: 10.1002/advs.201500369
Rights: © 2016 The Authors. Published by WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:MSE Journal Articles

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