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NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque‐competence, Aβ(1–40)ox and Aβ(1–42)ox
Open accessAbstract
NMR studies of amyloid β‐peptides (Aβ) in aqueous solution provide a novel way in which to characterize the apparent Alzheimer’s disease‐related conformational polymorphism of Aβ. In the aqueous medium, neither of the polypeptides Aβ(1–40)ox or Aβ(1–42)ox (both of which contain a methionine sulfoxide at position 35) is folded into a globular structure, but they both deviate from random coil behavior by local conformational preferences of several short segments along the amino‐acid sequence. Differences between the solution structures of Aβ(1–40)ox and Aβ(1–42)ox are indicated only by decreased flexibility of the region from about residue 32 to the C‐terminus in Aβ(1–42)ox when compared to Aβ(1–40)ox. The lack of the observation of more extensive conformational differences between the two molecules is intriguing, considering that Aβ(1–42)ox in aqueous solution has much higher plaque‐competence than Aβ(1–40)ox.
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Amyloid plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431
Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022
Citron, M., Oltersdorf, T., Haass, C., McConlogue, L., Hung, A. Y., Seubert, P., Vigo-Pelfrey, C., Lieberburg, I., & Selkoe, D. J. (1992) · Nature · doi:10.1038/360672a0 · Cited by 1,757
Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs.
Burdick, D., Soreghan, B., Kwon, M., Kosmoski, J., Knauer, M., Henschen, A., Yates, J., Cotman, C., & Glabe, C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48529-8 · Cited by 1,014
Cited by
Gaggelli, E., Kozlowski, H., Valensin, D., & Valensin, G. (2006) · Chemical Reviews · doi:10.1021/cr040410w · Cited by 1,729
Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid Fibrils
Petkova, A. T., Yau, W.-M., & Tycko, R. (2006) · Biochemistry · doi:10.1021/bi051952q · Cited by 1,044
Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide
Faller, P., & Hureau, C. (2009) · Dalton Trans. · doi:10.1039/b813398k · Cited by 530
Tomaselli, S., Esposito, V., Vangone, P., van Nuland, N. A. J., Bonvin, A. M. J. J., Guerrini, R., Tancredi, T., Temussi, P. A., & Picone, D. (2006) · ChemBioChem · doi:10.1002/cbic.200500223 · Cited by 438
Atomic-resolution dynamics on the surface of amyloid-β protofibrils probed by solution NMR
Fawzi, N. L., Ying, J., Ghirlando, R., Torchia, D. A., & Clore, G. M. (2011) · Nature · doi:10.1038/nature10577 · Cited by 419
Metadata
- Authors
- Riek, R., Güntert, P., Döbeli, H., Wipf, B., & Wüthrich, K.
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 2001-11-15
- Volume
- 268
- Issue
- 22
- Pages
- 5930-5936
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W1595368494
- Cited by
- 221
- References
- 4
- FWCI
- 3.13
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Riek, R., Güntert, P., Döbeli, H., Wipf, B., & Wüthrich, K. (2001). NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque‐competence, Aβ(1–40)ox and Aβ(1–42)ox. European Journal of Biochemistry. https://doi.org/10.1046/j.0014-2956.2001.02537.x
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.