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Single-Molecule Imaging of Amyloid-β Protein (Aβ) of Alzheimerĺs Disease: From Single-Molecule Structures to Aggregation Mechanisms and Membrane Interactions


Aguilar, M-I and Hou, X and Losic, D and Mechler, AI and Martin, LL and Small, DH, Single-Molecule Imaging of Amyloid-β Protein (Aβ) of Alzheimer's Disease: From Single-Molecule Structures to Aggregation Mechanisms and Membrane Interactions, Bio-nanoimaging: Protein Misfolding & Aggregation, Elsevier, Uversky VN and Lyubchenko YL (ed), United States of America, pp. 47-56. ISBN 978-0-12-394431-3 (2014) [Research Book Chapter]

Copyright Statement

Copyright 2014 Elsevier Inc.

DOI: doi:10.1016/B978-0-12-394431-3.00005-5


Recent advances in single-molecule imaging have allowed unprecedented insight into the structure of biomolecules and, consequently, into the role the structure plays in biochemical processes. A particular process of interest is the aggregation of the amyloid╬▓ protein (A╬▓ ), which is thought to be an important step in the pathogenesis of Alzheimer's disease: there is increasing evidence that A╬▓ oligomers may be the neurotoxic species in vivo. However, little is known about the structural organization of small A╬▓ oligomers. While an increasing number of studies report the atomic-level modeling of A╬▓ aggregation, there is still significant controversy over the specific architecture of A╬▓ oligomers and fibrils. The use of scanning probe microscopy techniques, including scanning tunneling microscopy (STM) and atomic force microscopy (AFM), may be able to bridge this gap in knowledge. Complementary microscopy techniques can reveal internal structure in many A╬▓ monomers, consistent with a conformation in which the polypeptide chain is folded into 2, 3 or 4 domains. In this chapter, we review the most recent studies on the high-resolution imaging of A╬▓, and we re-examine different models of A╬▓ aggregation, fibril formation and membrane interactions. ┬ę 2014 Elsevier Inc. All rights reserved..

Item Details

Item Type:Research Book Chapter
Research Division:Biomedical and Clinical Sciences
Research Group:Neurosciences
Research Field:Neurosciences not elsewhere classified
Objective Division:Health
Objective Group:Clinical health
Objective Field:Clinical health not elsewhere classified
UTAS Author:Small, DH (Professor David Small)
ID Code:98499
Year Published:2014
Deposited By:Menzies Institute for Medical Research
Deposited On:2015-02-18
Last Modified:2017-11-06

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