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Flexible N-Termini of Amyloid beta-Protein Oligomers: A Link between Structure and Activity?
Journal article   Peer reviewed

Flexible N-Termini of Amyloid beta-Protein Oligomers: A Link between Structure and Activity?

Brigita Urbanc
Israel journal of chemistry, v 57(7-8), pp 651-664
01 Jul 2017
DOI: https://doi.org/10.1002/ijch.201600097
Featured in Collection :   UN Sustainable Development Goals @ Drexel

Abstract

Chemistry Chemistry, Multidisciplinary Physical Sciences Science & Technology
Revised amyloid cascade hypothesis of Alzheimers disease (AD) states that amyloid -protein (A) triggers the disease through formation of soluble low molecular weight (LMW) assemblies, called oligomers, which are challenging to characterize experimentally as well as computationally due to their heterogeneous and polymorphic nature, lack of ordered structure, and short lifetimes. Recent findings challenge the view of A oligomers as exclusively toxic entities by revealing their dual, protective and disruptive nature in the context of immune response and AD, respectively. In this review, the understanding of A oligomer formation and structure is discussed from the AD perspective. The structure-activity relationship (SAR) that implicates flexible, solvent exposed N-termini of A oligomers, observed in computer simulations, in mediating their toxic as well as protective activity is proposed.

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8 citations in Web of Science
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UN Sustainable Development Goals (SDGs)

This publication has contributed to the advancement of the following goals:

#3 Good Health and Well-Being

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Web of Science research areas
Chemistry, Multidisciplinary
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