The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Controlling Amyloid β-Peptide Fibril Formation with Protease-stable Ligands
Open accessAbstract
We have previously shown that short peptides incorporating the sequence KLVFF can bind to the approximately 40amino acid residue Alzheimer amyloid beta-peptide (Abeta) and disrupt amyloid fibril formation (Tjernberg, L. O., Näslund, J., Lindqvist, F., Johansson, J., Karlström, A. R., Thyberg, J., Terenius, L., and Nordstedt, C. (1996) J. Biol. Chem. 271, 8545-8548). Here, it is shown that KLVFF binds stereospecifically to the homologous sequence in Abeta (i.e. Abeta16-20). Molecular modeling suggests that association of the two homologous sequences leads to the formation of an atypical anti-parallel beta-sheet structure stabilized primarily by interaction between the Lys, Leu, and COOH-terminal Phe. By screening combinatorial pentapeptide libraries exclusively composed of D-amino acids, several ligands with a general motif containing phenylalanine in the second position and leucine in the third position were identified. Ligands composed of D-amino acids were not only capable of binding Abeta but also prevented formation of amyloid-like fibrils. These ligands are protease-resistant and may thus be useful as experimental agents against amyloid fibril formation in vivo.
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The chemistry of Alzheimer’s disease
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Nanotechnologies for Alzheimer's disease: diagnosis, therapy, and safety issues
Brambilla, D., Le Droumaguet, B., Nicolas, J., Hashemi, S. H., Wu, L.-P., Moghimi, S. M., Couvreur, P., & Andrieux, K. (2011) · Nanomedicine: Nanotechnology, Biology and Medicine · doi:10.1016/j.nano.2011.03.008 · Cited by 294
Inhibitors of Amyloid Toxicity Based on β-sheet Packing of Aβ40 and Aβ42
Sato, T., Kienlen-Campard, P., Ahmed, M., Liu, W., Li, H., Elliott, J. I., Aimoto, S., Constantinescu, S. N., Octave, J.-N., & Smith, S. O. (2006) · Biochemistry · doi:10.1021/bi052485f · Cited by 191
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Rauk, A. (2008) · Dalton Transactions · doi:10.1039/b718601k · Cited by 139
Oxidation of Aβ and Plaque Biogenesis in Alzheimer's Disease and Down Syndrome
Head, E., Garzon-Rodriguez, W., Johnson, J. K., Lott, I. T., Cotman, C. W., & Glabe, C. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2001.0431 · Cited by 75
Metadata
- Authors
- Tjernberg, L. O., Lilliehöök, C., Callaway, D. J. E., Näslund, J., Hahne, S., Thyberg, J., Terenius, L., & Nordstedt, C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-05
- Volume
- 272
- Issue
- 19
- Pages
- 12601-12605
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2165383180
- Cited by
- 231
- References
- 11
- FWCI
- 4.78
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Tjernberg, L. O., Lilliehöök, C., Callaway, D. J. E., Näslund, J., Hahne, S., Thyberg, J., Terenius, L., & Nordstedt, C. (1997). Controlling Amyloid β-Peptide Fibril Formation with Protease-stable Ligands. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.272.19.12601
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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.
