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Issue 30, 2013
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Hydrogen bonding involving side chain exchangeable groups stabilizes amyloid quarternary structure

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Abstract

The amyloid β-peptide (Aβ) is the major structural component of amyloid fibrils in the plaques of brains of Alzheimer's disease patients. Numerous studies have addressed important aspects of secondary and tertiary structure of fibrils. In electron microscopic images, fibrils often bundle together. The mechanisms which drive the association of protofilaments into bundles of fibrils are not known. We show here that amino acid side chain exchangeable groups like e.g. histidines can provide useful restraints to determine the quarternary assembly of an amyloid fibril. Exchangeable protons are only observable if a side chain hydrogen bond is formed and the respective protons are protected from exchange. The method relies on deuteration of the Aβ peptide. Exchangeable deuterons are substituted with protons, before fibril formation is initiated.

Graphical abstract: Hydrogen bonding involving side chain exchangeable groups stabilizes amyloid quarternary structure

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Publication details

The article was received on 22 Dec 2012, accepted on 07 May 2013 and first published on 08 May 2013


Article type: Paper
DOI: 10.1039/C3CP44653K
Citation: Phys. Chem. Chem. Phys., 2013,15, 12551-12557
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    Hydrogen bonding involving side chain exchangeable groups stabilizes amyloid quarternary structure

    V. Agarwal, R. Linser, M. Dasari, U. Fink, J. L. del Amo and B. Reif, Phys. Chem. Chem. Phys., 2013, 15, 12551
    DOI: 10.1039/C3CP44653K

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