Socher E, Sticht H, Horn A (2014)
Publication Status: Published
Publication Type: Journal article, Original article
Publication year: 2014
Publisher: American Chemical Society
Book Volume: 5
Pages Range: 161-167
Journal Issue: 3
DOI: 10.1021/cn400208r
The amyloid-β (Aβ) peptide is one key molecule in the pathogenesis of Alzheimer's disease. We investigated the conformational stability of a nonfibrillar tetrameric Aβ structure by molecular dynamics (MD) simulations revealing that the stability of the Aβ tetramer depends critically on the C-terminal length. In contrast to the Aβ tetramer, which proved to be instable, the simulations demonstrate structural integrity of the Aβ and Aβ tetramers. These differences in stability can be attributed to an extension of the middle strand of a three-stranded antiparallel β sheet through residues 41-43, only present in the longer Aβ species that aggregate faster and are more neurotoxic. Additional MD simulations demonstrate that this higher stability is also present in the monomers forming the tetramer. In conclusion, our findings suggest the existence of a nonfibrillar oligomer topology that is significantly more stable for the longer Aβ species, thus offering a structural explanation for their higher neurotoxicity. © 2014 American Chemical Society.
APA:
Socher, E., Sticht, H., & Horn, A. (2014). The conformational stability of nonfibrillar amyloid-β peptide oligomers critically depends on the C-terminal peptide length. ACS Chemical Neuroscience, 5(3), 161-167. https://doi.org/10.1021/cn400208r
MLA:
Socher, Eileen, Heinrich Sticht, and Anselm Horn. "The conformational stability of nonfibrillar amyloid-β peptide oligomers critically depends on the C-terminal peptide length." ACS Chemical Neuroscience 5.3 (2014): 161-167.
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