A “cross-stitched” peptide with improved helicity and proteolytic stability
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Peptide “cross-stitching” maintains binding affinity and can enhance helical and proteolytic stability.
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Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design.
Marqusee, S., & Baldwin, R. L. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.24.8898 · Cited by 955 · see citing works
Chang, Y. S., Graves, B. J., Guerlavais, V., Tovar, C., Packman, K. E., To, K.-H., Olson, K. A., Kesavan, K. P., Gangurde, P., Mukherjee, A., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303002110 · Cited by 666 · see citing works
Luo, P., & Baldwin, R. L. (1997) · Biochemistry · doi:10.1021/bi9707133 · Cited by 643 · see citing works
Peptide stapling techniques based on different macrocyclisation chemistries
Lau, Y. H., de Andrade, P., Wu, Y., & Spring, D. R. (2014) · Chemical Society Reviews · doi:10.1039/c4cs00246f · Cited by 593 · see citing works
The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer
Stewart, M. L., Fire, E., Keating, A. E., & Walensky, L. D. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.391 · Cited by 418 · see citing works
Peptide Antagonists of the Human Estrogen Receptor
Norris, J. D., Paige, L. A., Christensen, D. J., Chang, C., Huacani, M. R., Fan, D., Hamilton, P. T., Fowlkes, D. M., & McDonnell, D. P. (1999) · Science · doi:10.1126/science.285.5428.744 · Cited by 367 · see citing works
Chang, C., Norris, J. D., Grøn, H., Paige, L. A., Hamilton, P. T., Kenan, D. J., Fowlkes, D. M., & McDonnell, D. P. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.12.8226 · Cited by 366 · see citing works
Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic
Bird, G. H., Madani, N., Perry, A. F., Princiotto, A. M., Supko, J. G., He, X., Gavathiotis, E., Sodroski, J., & Walensky, L. D. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002713107 · Cited by 345 · see citing works
Design and Structure of Stapled Peptides Binding to Estrogen Receptors
Phillips, C., Roberts, L. R., Schade, M., Bazin, R., Bent, A., Davies, N. L., Moore, R., Pannifer, A. D., Pickford, A. R., Prior, S. H., et al. (2011) · Journal of the American Chemical Society · doi:10.1021/ja202946k · Cited by 247 · see citing works
Comparative α‐Helicity of Cyclic Pentapeptides in Water
de Araujo, A. D., Hoang, H. N., Kok, W. M., Diness, F., Gupta, P. K., Hill, T. A., Driver, R. W., Price, D. A., Liras, S. I., & Fairlie, D. P. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201310245 · Cited by 177 · see citing works
Stitched α-Helical Peptides via Bis Ring-Closing Metathesis
Hilinski, G. J., Kim, Y., Hong, J., Kutchukian, P. S., Nartey, C. M., Berkovitch, S. S., Chang, A. T., Ham, S., & Verdine, G. L. (2014) · Journal of the American Chemical Society · doi:10.1021/ja505141j · Cited by 163 · see citing works
Energetic contribution of solvent-exposed ion pairs to alpha-helix structure
Lyu, P. C., Gans, P. J., & Kallenbach, N. R. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90735-3 · Cited by 120 · see citing works
Geistlinger, T. R., & Guy, R. K. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0348391 · Cited by 94 · see citing works
Speltz, T. E., Fanning, S. W., Mayne, C. G., Fowler, C. E., Tajkhorshid, E., Greene, G. L., & Moore, T. W. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201510557 · Cited by 89 · see citing works
Self-citationPotent Inhibitors of LXXLL‐Based Protein–Protein Interactions
Galande, A. K., Bramlett, K. S., Trent, J. O., Burris, T. P., Wittliff, J. L., & Spatola, A. F. (2005) · ChemBioChem · doi:10.1002/cbic.200500083 · Cited by 86 · see citing works
Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase
Cromm, P. M., Spiegel, J., Küchler, P., Dietrich, L., Kriegesmann, J., Wendt, M., Goody, R. S., Waldmann, H., & Grossmann, T. N. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00386 · Cited by 82 · see citing works
Moradi, M., & Tajkhorshid, E. (2014) · Journal of Chemical Theory and Computation · doi:10.1021/ct5002285 · Cited by 74 · see citing works
Self-citationBicyclic Helical Peptides as Dual Inhibitors Selective for Bcl2A1 and Mcl-1 Proteins
de Araujo, A. D., Lim, J., Wu, K., Xiang, Y., Good, A. C., Skerlj, R. T., & Fairlie, D. P. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00010 · Cited by 60 · see citing works
Raj, G. V., Sareddy, G. R., Ma, S., Lee, T.-K., Viswanadhapalli, S., Li, R., Liu, X., Murakami, S., Chen, C.-C., Lee, W.-R., et al. (2017) · eLife · doi:10.7554/elife.26857 · Cited by 58 · see citing works
Douse, C. H., Maas, S. J., Thomas, J. C., Garnett, J. A., Sun, Y., Cota, E., & Tate, E. W. (2014) · ACS Chemical Biology · doi:10.1021/cb500271c · Cited by 56 · see citing works
Gunther, J. R., Du, Y., Rhoden, E. E., Lewis, I., Revennaugh, B., Moore, T. W., Kim, S. H., Dingledine, R. J., Fu, H., & Katzenellenbogen, J. A. (2009) · SLAS DISCOVERY · doi:10.1177/1087057108329349 · Cited by 55 · see citing works
Self-citationA Short Double-Stapled Peptide Inhibits Respiratory Syncytial Virus Entry and Spreading
Gaillard, V., Galloux, M., Garcin, D., Eléouët, J., Goffic, R. L., Larcher, T., Rameix‐Welti, M., Boukadiri, A., Héritier, J., Segura, J., et al. (2017) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02241-16 · Cited by 54 · see citing works
Proline primed helix length as a modulator of the nuclear receptor-coactivator interaction
Fuchs, S., Nguyen, H. D., Phan, T. T. P., Burton, M. F., Nieto, L., de Vries-van Leeuwen, I. J., Schmidt, A., Goodarzifard, M., Agten, S. M., Rose, R., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja311748r · Cited by 43 · see citing works
Comparative α‐Helicity of Cyclic Pentapeptides in Water
de Araujo, A. D., Hoang, H. N., Kok, W. M., Diness, F., Gupta, P. K., Hill, T. A., Driver, R. W., Price, D. A., Liras, S. I., & Fairlie, D. P. (2014) · Angewandte Chemie · doi:10.1002/ange.201310245 · Cited by 43 · see citing works
A Cell-Permeable Stapled Peptide Inhibitor of the Estrogen Receptor/Coactivator Interaction
Speltz, T. E., Danes, J. M., Stender, J. D., Frasor, J. M., & Moore, T. W. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.7b01016 · Cited by 42 · see citing works
Self-citationXie, M., Zhao, H., Liu, Q., Zhu, Y., Yin, F., Liang, Y., Jiang, Y., Wang, D., Hu, K., Qin, X., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00732 · Cited by 41 · see citing works
Jiang, Y., Hu, K., Shi, X., et al. (2016) · Organic & Biomolecular Chemistry · doi:10.1039/c6ob02289h · Cited by 25 · see citing works
Hu, K., Sun, C., Yang, D., et al. (2017) · Chemical Communications · doi:10.1039/c7cc03799f · Cited by 16 · see citing works
Development of a potent peptide inhibitor of estrogen receptor α
Qin, X., Zhao, H., Jiang, Y., et al. (2018) · Chinese Chemical Letters · doi:10.1016/j.cclet.2018.04.004 · Cited by 12 · see citing works
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Molecular insights into the role of Estrogen Receptor Beta in Ecdysterone Mediated Anabolic Activity
Tariq, S. S., Sardar, M., Shafiq, M., Heinz, H., Nur-e-Alam, M., Ahmed, A., & Ul-Haq, Z. (2025) · PLoS One · doi:10.1371/journal.pone.0320865 · Cited by 4 · see citing works
“The structures of these proteins, retrieved from the Protein Data Bank with the PDB IDs 2YHD [12], 5WGD [13] and 4J26 [14] respectively, to serve as the preliminary point for further analysis.”
- Authors
- Speltz, T. E., Mayne, C. G., Fanning, S. W., Siddiqui, Z., Tajkhorshid, E., Greene, G. L., & Moore, T. W.
- Affiliations
- University of Illinois Chicago (US)
- University of Illinois Urbana-Champaign (US)
- University of Chicago (US)
- Corresponding author
- Moore, Terry W.
- ORCID
- Venue
- Organic & Biomolecular Chemistry
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2018
- Volume
- 16
- Issue
- 20
- Pages
- 3702-3706
- ISSN
- 1477-0520 (ISSN-L)
- 1477-0539
- PMC
- PMC5993042
- OpenAlex
- W2802585333
- Cited by
- 39
- References
- 29
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 6 · 2023: 3 · 2022: 2 · 2021: 2 · 2020: 7 · 2019: 9 · 2018: 1
- FWCI
- 1.69
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Organic & Biomolecular Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (P41-GM104601, T32AT007533)
- National Science Foundation (ACI-1548562, TG-MCA06N060, TG-MCB170062)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Keywords
- peptide design, proteolytic stability, estrogen receptor alpha, peptide-receptor binding, computational peptide design
- MeSH terms
- Protein Conformation, alpha-Helical, Amino Acid Sequence, Binding Sites, Models, Molecular, Peptides, Amino Acid Motifs, Estrogen Receptor alpha, Proteolysis
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