The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Sequence-Selective Recognition of Peptides within the Single Binding Pocket of a Self-Assembled Coordination Cage
Abstract
The single binding pocket of a self-assembled Pd6L4 coordination cage recognizes oligopeptides in a highly sequence-selective fashion. In particular, the Trp-Trp-Ala sequence is strongly bound by the cavity (Ka >/=106 M-1). Tripeptides possessing the same residues but in different sequences (i.e., Trp-Ala-Trp and Ala-Trp-Trp) show much poorer affinity. Even singly mutated tripeptides with aromatic-aromatic-aliphatic sequences of the residues (e.g., Trp-Trp-Gly and Trp-Tyr-Ala) are not recognized efficiently. X-ray analysis and NMR reveal that all residues of the Trp-Trp-Ala sequence cooperatively interact with the cage via CH-pi and pi-pi 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
Cited by
Supramolecular Chemistry in Water
Oshovsky, G. V., Reinhoudt, D. N., & Verboom, W. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200602815 · Cited by 708
Functional behaviour from controlled self-assembly: challenges and prospects
Ward, M. D., & Raithby, P. R. (2013) · Chem. Soc. Rev. · doi:10.1039/c2cs35123d · Cited by 444
Inducing α-Helices in Short Oligopeptides through Binding by an Artificial Hydrophobic Cavity
Dolain, C., Hatakeyama, Y., Sawada, T., Tashiro, S., & Fujita, M. (2010) · Journal of the American Chemical Society · doi:10.1021/ja100585w · Cited by 45
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Metadata
- Authors
- Tashiro, S., Tominaga, M., Kawano, M., Therrien, B., Ozeki, T., & Fujita, M.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2005-03-09
- Volume
- 127
- Issue
- 13
- Pages
- 4546-4547
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2000513559
- Cited by
- 171
- References
- 1
- FWCI
- 8.14
- Type
- journal article
- Language
- en
- Open access
- closed
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