The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Probing the α‐Helical Structural Stability of Stapled p53 Peptides: Molecular Dynamics Simulations and Analysis
Abstract
Reactivation of the p53 cell apoptosis pathway through inhibition of the p53‐hDM2 interaction is a viable approach to suppress tumor growth in many human cancers and stabilization of the helical structure of synthetic p53 analogs via a hydrocarbon cross‐link (staple) has been found to lead to increased potency and inhibition of protein–protein binding (J. Am. Chem. Soc. 129: 5298). However, details of the structure and dynamic stability of the stapled peptides are not well understood. Here, we use extensive all‐atom molecular dynamics simulations to study a series of stapled α‐helical peptides over a range of temperatures in solution. The peptides are found to exhibit substantial variations in predicted α‐helical propensities that are in good agreement with the experimental observations. In addition, we find significant variation in local structural flexibility of the peptides with the position of the linker, which appears to be more closely related to the observed differences in activity than the absolute α‐helical stability. These simulations provide new insights into the design of α‐helical stapled peptides and the development of potent inhibitors of α‐helical protein–protein interfaces.
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Citations
Cites
Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206
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
Direct inhibition of the NOTCH transcription factor complex
Moellering, R. E., Cornejo, M., Davis, T. N., Bianco, C. D., Aster, J. C., Blacklow, S. C., Kung, A. L., Gilliland, D. G., Verdine, G. L., & Bradner, J. E. (2009) · Nature · doi:10.1038/nature08543 · Cited by 752
Dual role of proapoptotic BAD in insulin secretion and beta cell survival
Danial, N. N., Walensky, L. D., Zhang, C.-Y., Choi, C. S., Fisher, J. K., Molina, A. J. A., Datta, S. R., Pitter, K. L., Bird, G. H., Wikstrom, J. D., et al. (2008) · Nature Medicine · doi:10.1038/nm1717 · Cited by 307
Cited by
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
Chemical modulation of chaperone-mediated autophagy by retinoic acid derivatives
Anguiano, J., Garner, T. P., Mahalingam, M., Das, B. C., Gavathiotis, E., & Cuervo, A. M. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1230 · Cited by 222
Clark, A. J., Gindin, T., Zhang, B., Wang, L., Abel, R., Murret, C. S., Xu, F., Bao, A., Lu, N. J., Zhou, T., et al. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.11.021 · Cited by 96
Allosteric inhibition of antiapoptotic MCL-1
Lee, S., Wales, T. E., Escudero, S., Cohen, D. T., Luccarelli, J., Gallagher, C. G., Cohen, N. A., Huhn, A. J., Bird, G. H., Engen, J. R., et al. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3223 · Cited by 59
Grover, A., Katiyar, S. P., Jeyakanthan, J., Dubey, V. K., & Sundar, D. (2012) · BMC Genomics · doi:10.1186/1471-2164-13-s7-s20 · Cited by 52
Metadata
- Authors
- Guo, Z., Mohanty, U., Noehre, J., Sawyer, T. K., Sherman, W., & Krilov, G.
- Venue
- Chemical Biology & Drug Design
- Publisher
- Wiley
- Published
- 2010-02-22
- Volume
- 75
- Issue
- 4
- Pages
- 348-359
- ISSN
- 1747-0277 (ISSN-L)
- 1747-0285
- OpenAlex
- W1986876979
- Cited by
- 384
- References
- 4
- FWCI
- 4.02
- Type
- journal article
- Language
- en
- Open access
- closed
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