The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Contemporary strategies for the stabilization of peptides in the α-helical conformation
Open accessAbstract
Summary of recent advances Herein we review contemporary synthetic and protein design strategies to stabilize the α-helical motif in short peptides and miniature proteins. Advances in organometallic catalyst design, specifically for the olefin metathesis reaction, enable the use of hydrocarbon bridges to either crosslink side chains of specific residues or mimic intramolecular hydrogen bonds with carbon-carbon bonds. The resulting hydrocarbon-stapled and hydrogen bond surrogate α-helices provide unique synthetic ligands for targeting biomolecules. In the protein design realm, several classes of miniature proteins that display stable helical domains have been engineered and manipulated with powerful in vitro selection technologies to yield libraries of sequences that retain their helical folds. Rational re-design of these scaffolds provide distinctive reagents for the modulation of protein-protein interactions.
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Cites
Principles of protein-protein interactions
Jones, S., & Thornton, J. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.13 · Cited by 2,684
Activation of Apoptosis in Vivo by a Hydrocarbon-Stapled BH3 Helix
Walensky, L. D., Kung, A. L., Escher, I., Malia, T. J., Barbuto, S., Wright, R. D., Wagner, G., Verdine, G. L., & Korsmeyer, S. J. (2004) · Science · doi:10.1126/science.1099191 · Cited by 1,349
Schafmeister, C. E., Po, J., & Verdine, G. L. (2000) · Journal of the American Chemical Society · doi:10.1021/ja000563a · Cited by 1,037
Designing a 20-residue protein
Neidigh, J. W., Fesinmeyer, R. M., & Andersen, N. H. (2002) · Nature Structural Biology · doi:10.1038/nsb798 · Cited by 793
General approach to the synthesis of short .alpha.-helical peptides
Jackson, D. Y., King, D. S., Chmielewski, J., Singh, S., & Schultz, P. G. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00024a067 · Cited by 313
Leduc, A.-M., Trent, J. O., Wittliff, J. L., Bramlett, K. S., Briggs, S. L., Chirgadze, N. Y., Wang, Y., Burris, T. P., & Spatola, A. F. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1934759100 · Cited by 222
Geistlinger, T. R., & Guy, R. K. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0348391 · Cited by 94
Cited by
Small molecules, big targets: drug discovery faces the protein–protein interaction challenge
Scott, D. E., Bayly, A. R., Abell, C., & Skidmore, J. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.29 · Cited by 1,137
Future directions for peptide therapeutics development
Kaspar, A. A., & Reichert, J. M. (2013) · Drug Discovery Today · doi:10.1016/j.drudis.2013.05.011 · Cited by 750
Inhibition of α-helix-mediated protein–protein interactions using designed molecules
Azzarito, V., Long, K., Murphy, N. S., & Wilson, A. J. (2013) · Nature Chemistry · doi:10.1038/nchem.1568 · Cited by 727
Modulators of Protein–Protein Interactions
Milroy, L.-G., Grossmann, T. N., Hennig, S., Brunsveld, L., & Ottmann, C. (2014) · Chemical Reviews · doi:10.1021/cr400698c · Cited by 497
Stapled Peptides for Intracellular Drug Targets
Verdine, G. L., & Hilinski, G. J. (2012) · Methods in Enzymology · doi:10.1016/b978-0-12-396962-0.00001-x · Cited by 433
Metadata
- Authors
- Henchey, L. K., Jochim, A. L., & Arora, P. S.
- Venue
- Current Opinion in Chemical Biology
- Publisher
- Elsevier BV
- Published
- 2008-12
- Volume
- 12
- Issue
- 6
- Pages
- 692-697
- ISSN
- 1367-5931 (ISSN-L)
- OpenAlex
- W2023697479
- Cited by
- 288
- References
- 7
- FWCI
- 0.95
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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