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Chimeric (α/β + α)-Peptide Ligands for the BH3-Recognition Cleft of Bcl-x L : Critical Role of the Molecular Scaffold in Protein Surface Recognition
Abstract
Molecules that bind to specific surface sites on proteins are of great interest from both fundamental and practical perspectives. We are exploring a ligand development strategy that is based on oligomers with discrete folding propensities ("foldamers"); we target a specific cleft on the cancer-associated protein Bcl-xL because this system is well characterized structurally. In vivo, this cleft binds to alpha-helical segments (BH3 domains) of other proteins. We evaluated several types of helical foldamer, built entirely from beta-amino acid residues or from mixtures of alpha- and beta-amino acid residues, and ultimately identified foldamers in the latter class that bind very tightly to Bcl-xL. Our results suggest that combining different types of foldamer backbones will be an effective and general strategy for creating high-affinity and specific ligands for protein surface sites.
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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
Small-molecule inhibitors of protein–protein interactions: progressing towards the dream
Arkin, M. R., & Wells, J. A. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1343 · Cited by 1,705
TGF-ß Signaling in Fibroblasts Modulates the Oncogenic Potential of Adjacent Epithelia
Bhowmick, N. A., Chytil, A., Plieth, D., Gorska, A. E., Dumont, N., Shappell, S., Washington, M. K., Neilson, E. G., & Moses, H. L. (2004) · Science · doi:10.1126/science.1090922 · Cited by 1,401
A Protein-Counting Mechanism for Telomere Length Regulation in Yeast
Marcand, S., Gilson, E., & Shore, D. (1997) · Science · doi:10.1126/science.275.5302.986 · Cited by 524
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
Bcl-2-regulated apoptosis: mechanism and therapeutic potential
Adams, J. M., & Cory, S. (2007) · Current Opinion in Immunology · doi:10.1016/j.coi.2007.05.004 · Cited by 658
Vasudev, P. G., Chatterjee, S., Shamala, N., & Balaram, P. (2011) · Chemical Reviews · doi:10.1021/cr100100x · Cited by 329
Metadata
- Authors
- Sadowsky, J. D., Schmitt, M. A., Lee, H.-S., Umezawa, N., Wang, S., Tomita, Y., & Gellman, S. H.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2005-08-01
- Volume
- 127
- Issue
- 34
- Pages
- 11966-11968
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2090909356
- Cited by
- 173
- References
- 4
- FWCI
- 6.45
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Chimeric (α/β + α)-Peptide Ligands for the BH3-Recognition Cleft of Bcl-x L : Critical Role of the Molecular Scaffold in Protein Surface Recognition. https://app.cochat.ai/papers/10.1021/ja053678t
- The paper
- Sadowsky, J. D., Schmitt, M. A., Lee, H.-S., Umezawa, N., Wang, S., Tomita, Y., & Gellman, S. H. (2005). Chimeric (α/β + α)-Peptide Ligands for the BH3-Recognition Cleft of Bcl-x L : Critical Role of the Molecular Scaffold in Protein Surface Recognition. Journal of the American Chemical Society. https://doi.org/10.1021/ja053678t
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