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  Hydrogen bonding involving side chain exchangeable groups stabilizes amyloid quarternary structure.

Agarwal, V., Linser, R., Dasari, M., Fink, U., Lopez del Amo, J. M., & Reif, B. (2013). Hydrogen bonding involving side chain exchangeable groups stabilizes amyloid quarternary structure. Physical Chemistry Chemical Physics, 15(30), 12551-12557. doi:10.1039/c3cp44653k.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0018-A044-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-4213-3
Genre: Journal Article

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1977452.pdf (Publisher version), 3MB
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 Creators:
Agarwal, V., Author
Linser, R.1, Author              
Dasari, M., Author
Fink, U., Author
Lopez del Amo, J. M., Author
Reif, B., Author
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1Research Group of Solid-State NMR-2, MPI for Biophysical Chemistry, Max Planck Society, ou_1950286              

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 Abstract: The amyloid beta-peptide (A beta) 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 A beta peptide. Exchangeable deuterons are substituted with protons, before fibril formation is initiated.

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Language(s): eng - English
 Dates: 2013-05-082013
 Publication Status: Published in print
 Pages: -
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 Rev. Method: Peer
 Identifiers: DOI: 10.1039/c3cp44653k
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Title: Physical Chemistry Chemical Physics
Source Genre: Journal
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Pages: - Volume / Issue: 15 (30) Sequence Number: - Start / End Page: 12551 - 12557 Identifier: -