The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Cyclic and Macrocyclic Peptides as Chemical Tools To Recognise Protein Surfaces and Probe Protein–Protein Interactions
Open accessAbstract
Targeting protein surfaces and protein–protein interactions (PPIs) with small molecules is a frontier goal of chemical biology and provides attractive therapeutic opportunities in drug discovery. The molecular properties of protein surfaces, including their shallow features and lack of deep binding pockets, pose significant challenges, and as a result have proved difficult to target. Peptides are ideal candidates for this mission due to their ability to closely mimic many structural features of protein interfaces. However, their inherently low intracellular stability and permeability and high in vivo clearance have thus far limited their biological applications. One way to improve these properties is to constrain the secondary structure of linear peptides by cyclisation. Herein we review various classes of cyclic and macrocyclic peptides as chemical probes of protein surfaces and modulators of PPIs. The growing interest in this area and recent advances provide evidence of the potential of developing peptide‐like molecules that specifically target these interactions.
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Cites
In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661
Adding New Chemistries to the Genetic Code
Liu, C. C., & Schultz, P. G. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.052308.105824 · Cited by 1,725
Buckley, D. L., Van Molle, I., Gareiss, P. C., Tae, H. S., Michel, J., Noblin, D. J., Jorgensen, W. L., Ciulli, A., & Crews, C. M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja209924v · Cited by 569
Self-citationModulators 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
Structural basis for high-affinity peptide inhibition of p53 interactions with MDM2 and MDMX
Pazgier, M., Liu, M., Zou, G., Yuan, W., Li, C., Li, C., Li, J., Monbo, J., Zella, D., Tarasov, S. G., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900947106 · Cited by 391
Selection of peptides binding to the alpha 5 beta 1 integrin from phage display library.
Koivunen, E., Gay, D. A., & Ruoslahti, E. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80715-7 · Cited by 344
Small‐Molecule Inhibitors of the Interaction between the E3 Ligase VHL and HIF1α
Buckley, D. L., Gustafson, J. L., Van Molle, I., Roth, A. G., Tae, H. S., Gareiss, P. C., Jorgensen, W. L., Ciulli, A., & Crews, C. M. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201206231 · Cited by 302
Self-citationMiranda, E., Nordgren, I. K., Male, A. L., Lawrence, C. E., Hoakwie, F., Cuda, F., Court, W., Fox, K. R., Townsend, P. A., Packham, G. K., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja402993u · Cited by 185
Qian, Z., LaRochelle, J. R., Jiang, B., Lian, W., Hard, R. L., Selner, N. G., Luechapanichkul, R., Barrios, A. M., & Pei, D. (2014) · Biochemistry · doi:10.1021/bi5004102 · Cited by 176
Tavassoli, A., Lu, Q., Gam, J., Pan, H., Benkovic, S. J., & Cohen, S. N. (2008) · ACS Chemical Biology · doi:10.1021/cb800193n · Cited by 153
Birts, C. N., Nijjar, S. K., Mardle, C. A., Hoakwie, F., Duriez, P. J., Blaydes, J. P., & Tavassoli, A. (2013) · Chemical Science · doi:10.1039/c3sc50481f · Cited by 85
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Self-citationChen, K.-E., Guo, Q., Hill, T. A., Cui, Y., Kendall, A. K., Yang, Z., Hall, R. J., Healy, M. D., Sacharz, J., Norwood, S. J., et al. (2021) · Science Advances · doi:10.1126/sciadv.abg4007 · Cited by 34
Zhang, C., Xu, Z., Lin, K., Zhu, N., Zhang, C., Xu, W., Guo, J., Su, A., Li, C., & Duan, H. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c00227 · Cited by 12
Metadata
- Authors
- Cardote, T. A. F., & Ciulli, A.
- Venue
- ChemMedChem
- Publisher
- Wiley
- Published
- 2015-11-13
- Volume
- 11
- Issue
- 8
- Pages
- 787-794
- ISSN
- 1860-7179 (ISSN-L)
- 1860-7187
- OpenAlex
- W2101040826
- Cited by
- 186
- References
- 11
- FWCI
- 6.82
- Type
- journal article
- Language
- en
- Open access
- hybrid
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