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Pharmacological Profiles of Peptide Drug Candidates for the Treatment of Alzheimer's Disease
Open accessAbstract
Amyloid plaques in brain, composed of aggregates of amyloid-beta peptide, play a central role in the pathogenesis of Alzheimer's disease and represent a good target for treatment. We have shown previously that a 5-amino acid beta-sheet breaker peptide (iA beta 5p), end-protected, has the ability to induce a dramatic reduction in amyloid deposition in two different transgenic Alzheimer's models (Permanne, B., Adessi, C., Saborio, G. P., Fraga, S., Frossard, M.-J., Dewachter, I., Van Dorpe, J., Banks, W. A., Van Leuven, F., and Soto, C. (2002) FASEB J. 16, 860-862). The aim of this study was to evaluate the effect of chemical modifications of the peptide bonds at the metabolite cleavage sites on the pharmacological properties of iA beta 5p derivatives. Using a rational approach, peptide analogs were designed and tested for in vitro activity and enzymatic stability. One peptide analog containing a methyl group introduced at the nitrogen atom of one amide bond showed increased stability in vitro, a 10-fold higher in vivo half-life, and good brain uptake compared with iA beta 5p while maintaining a similar activity in vitro. Our results suggest that the pharmacological profile of beta-sheet breaker peptides can be improved to produce compounds with drug-like properties that might offer a new promise in the treatment of Alzheimer's disease.
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Cites
Arrest of -Amyloid Fibril Formation by a Pentapeptide Ligand
Tjernberg, L. O., Näslund, J., Lindqvist, F., Johansson, J., Karlström, A. R., Thyberg, J., Terenius, L., & Nordstedt, C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.15.8545 · Cited by 963
Murine tumor necrosis factor alpha is transported from blood to brain in the mouse
Gutierrez, E. G., Banks, W. A., & Kastin, A. J. (1993) · Journal of Neuroimmunology · doi:10.1016/0165-5728(93)90027-v · Cited by 577
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Cited by
Agrawal, M., Saraf, S., Saraf, S., Antimisiaris, S. G., Chougule, M. B., Shoyele, S. A., & Alexander, A. (2018) · Journal of Controlled Release · doi:10.1016/j.jconrel.2018.05.011 · Cited by 630
N‐Methylation of Peptides and Proteins: An Important Element for Modulating Biological Functions
Chatterjee, J., Rechenmacher, F., & Kessler, H. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201205674 · Cited by 494
Görbitz, C. H. (2006) · Chem. Commun. · doi:10.1039/b603080g · Cited by 437
Delivery of peptide and protein drugs over the blood–brain barrier
Brasnjevic, I., Steinbusch, H. W. M., Schmitz, C., & Martinez-Martinez, P. (2009) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2008.12.002 · Cited by 279
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
Metadata
- Authors
- Adessi, C., Frossard, M.-J., Boissard, C., Fraga, S., Bieler, S., Ruckle, T., Vilbois, F., Robinson, S. M., Mutter, M., Banks, W. A., & Soto, C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-04
- Volume
- 278
- Issue
- 16
- Pages
- 13905-13911
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2105818305
- Cited by
- 199
- References
- 2
- FWCI
- 6.33
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Adessi, C., Frossard, M.-J., Boissard, C., Fraga, S., Bieler, S., Ruckle, T., Vilbois, F., Robinson, S. M., Mutter, M., Banks, W. A., & Soto, C. (2003). Pharmacological Profiles of Peptide Drug Candidates for the Treatment of Alzheimer's Disease. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m211976200
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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.
