The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Amyloid β-Protein Monomer Folding: Free-Energy Surfaces Reveal Alloform-Specific Differences
Open accessAbstract
Alloform-specific differences in structural dynamics between Aβ40 and Aβ42 appear to underlie the pathogenesis of Alzheimer’s disease. To elucidate these differences, we performed µs time-scale replica exchange molecular dynamics simulations to sample the conformational space of the Aβ monomer and constructed its free energy surface. We find that neither peptide monomer is unstructured, but rather that each may be described as a unique statistical coil in which five relatively independent folding units exist, comprising residues 1–5, 10–13, 17–22, 28–37, and 39–42, which are connected by four turn structures. The free energy surfaces of both peptides are characterized by two large basins, comprising conformers either with substantial α-helix or β-sheet content. Conformational transitions within and between these basins are rapid. The two additional hydrophobic residues at the Aβ42 C-terminus, Ile41 and Ala42, significantly increase contacts within the C-terminus and between the C-terminus and the central hydrophobic cluster (Leu17-Ala21). As a result, the β-structure of Aβ42 is more stable than that of Aβ40 and the conformational equilibrium in Aβ42 shifts towards β-structure. These results suggest that drugs stabilizing α-helical Aβ conformers (or destabilizing the β-sheet state) would block formation of neurotoxic oligomers. The atomic-resolution conformer structures determined in our simulations may serve as useful targets for this purpose. The conformers also provide starting points for simulations of Aβ oligomerization, a process postulated to be the key pathogenetic event in AD.
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Amyloid Beta: Structure, Biology and Structure-Based Therapeutic Development
Chen, G.-F., Xu, T.-H., Yan, Y., Zhou, Y.-R., Jiang, Y., Melcher, K., & Xu, H. E. (2017) · Acta Pharmacologica Sinica · doi:10.1038/aps.2017.28 · Cited by 1,965
Assessing the Stability of Alzheimer’s Amyloid Protofibrils Using Molecular Dynamics
Lemkul, J. A., & Bevan, D. R. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp9110794 · Cited by 508
The chemistry of Alzheimer’s disease
Rauk, A. (2009) · Chemical Society Reviews · doi:10.1039/b807980n · Cited by 417
Amyloid β-protein oligomers and Alzheimer’s disease
Hayden, E. Y., & Teplow, D. B. (2013) · Alzheimer's Research & Therapy · doi:10.1186/alzrt226 · Cited by 276
Self-citationLin, Y.-S., Bowman, G. R., Beauchamp, K. A., & Pande, V. S. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2011.12.002 · Cited by 111
Metadata
- Authors
- Yang, M., & Teplow, D. B.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2008-12
- Volume
- 384
- Issue
- 2
- Pages
- 450-464
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2084187244
- Cited by
- 247
- References
- 12
- FWCI
- 9.65
- Type
- journal article
- Language
- en
- Open access
- green
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