The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
Peptoids that mimic the structure, function, and mechanism of helical antimicrobial peptides
Open accessAbstract
Antimicrobial peptides (AMPs) and their mimics are emerging as promising antibiotic agents. We present a library of “ampetoids” (antimicrobial peptoid oligomers) with helical structures and biomimetic sequences, several members of which have low-micromolar antimicrobial activities, similar to cationic AMPs like pexiganan. Broad-spectrum activity against six clinically relevant BSL2 pathogens is also shown. This comprehensive structure–activity relationship study, including circular dichroism spectroscopy, minimum inhibitory concentration assays, hemolysis and mammalian cell toxicity studies, and specular x-ray reflectivity measurements shows that the in vitro activities of ampetoids are strikingly similar to those of AMPs themselves, suggesting a strong mechanistic analogy. The ampetoids' antibacterial activity, coupled with their low cytotoxicity against mammalian cells, make them a promising class of antimicrobials for biomedical applications. Peptoids are biostable, with a protease-resistant N -substituted glycine backbone, and their sequences are highly tunable, because an extensive diversity of side chains can be incorporated via facile solid-phase synthesis. Our findings add to the growing evidence that nonnatural foldamers will emerge as an important class of therapeutics.
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Cites
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Gentilucci, L., De Marco, R., & Cerisoli, L. (2010) · Current Pharmaceutical Design · doi:10.2174/138161210793292555 · Cited by 586
A New Era of Antibiotics: The Clinical Potential of Antimicrobial Peptides
Browne, K., Chakraborty, S., Chen, R., Willcox, M. D., Black, D. S., Walsh, W. R., & Kumar, N. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197047 · Cited by 482
Park, S.-C., Park, Y., & Hahm, K.-S. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12095971 · Cited by 327
Ong, Z. Y., Wiradharma, N., & Yang, Y. Y. (2014) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2014.10.013 · Cited by 313
Mitochondrion-Targeting Peptides and Peptidomimetics: Recent Progress and Design Principles
Kim, S., Nam, H. Y., Lee, J., & Seo, J. (2020) · Biochemistry · doi:10.1021/acs.biochem.9b00857 · Cited by 75
Metadata
- Authors
- Chongsiriwatana, N. P., Patch, J. A., Czyzewski, A. M., Dohm, M. T., Ivankin, A., Gidalevitz, D., Zuckermann, R. N., & Barron, A. E.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2008-02-26
- Volume
- 105
- Issue
- 8
- Pages
- 2794-2799
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1993906884
- Cited by
- 657
- References
- 41
- FWCI
- 32.06
- Type
- journal article
- Language
- en
- Open access
- green
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- Chongsiriwatana, N. P., Patch, J. A., Czyzewski, A. M., Dohm, M. T., Ivankin, A., Gidalevitz, D., Zuckermann, R. N., & Barron, A. E. (2008). Peptoids that mimic the structure, function, and mechanism of helical antimicrobial peptides. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0708254105
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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