The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice
Open accessAbstract
The clinical translation of cationic α-helical antimicrobial peptides (AMPs) has been hindered by structural instability, proteolytic degradation and in vivo toxicity from nonspecific membrane lysis. Although analyses of hydrophobic content and charge distribution have informed the design of synthetic AMPs with increased potency and reduced in vitro hemolysis, nonspecific membrane toxicity in vivo continues to impede AMP drug development. Here, we analyzed a 58-member library of stapled AMPs (StAMPs) based on magainin II and applied the insights from structure–function–toxicity measurements to devise an algorithm for the design of stable, protease-resistant, potent and nontoxic StAMP prototypes. We show that a lead double-stapled StAMP named Mag(i+4)1,15(A9K,B21A,N22K,S23K) can kill multidrug-resistant Gram-negative pathogens, such as colistin-resistant Acinetobacter baumannii in a mouse peritonitis–sepsis model, without observed hemolysis or renal injury in murine toxicity studies. Inputting the amino acid sequences alone, we further generated membrane-selective StAMPs of pleurocidin, CAP18 and esculentin, highlighting the generalizability of our design platform. The authors designed stapled antimicrobial peptides that have potent antibacterial activity in mice and limited toxicity.
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Cites
Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
Brogden, K. A. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1098 · Cited by 5,829
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
Self-citationSchafmeister, C. E., Po, J., & Verdine, G. L. (2000) · Journal of the American Chemical Society · doi:10.1021/ja000563a · Cited by 1,037
Cited by
Gan, B. H., Gaynord, J., Rowe, S. M., Deingruber, T., & Spring, D. R. (2021) · Chemical Society Reviews · doi:10.1039/d0cs00729c · Cited by 511
Identification of antimicrobial peptides from the human gut microbiome using deep learning
Ma, Y., Guo, Z., Xia, B., Zhang, Y., Liu, X., Yu, Y., Tang, N., Tong, X., Wang, M., Ye, X., et al. (2022) · Nature Biotechnology · doi:10.1038/s41587-022-01226-0 · Cited by 490
Mode-of-Action of Antimicrobial Peptides: Membrane Disruption vs. Intracellular Mechanisms
Benfield, A. H., & Henriques, S. T. (2020) · Frontiers in Medical Technology · doi:10.3389/fmedt.2020.610997 · Cited by 367
DRAMP 3.0: an enhanced comprehensive data repository of antimicrobial peptides
Shi, G., Kang, X., Dong, F., Liu, Y., Zhu, N., Hu, Y., Xu, H., Lao, X., & Zheng, H. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab651 · Cited by 308
Huang, J., Xu, Y., Xue, Y., Huang, Y., Li, X., Chen, X., Xu, Y., Zhang, D., Zhang, P., Zhao, J., et al. (2023) · Nature Biomedical Engineering · doi:10.1038/s41551-022-00991-2 · Cited by 270
Metadata
- Authors
- Mourtada, R., Herce, H. D., Yin, D. J., Moroco, J. A., Wales, T. E., Engen, J. R., & Walensky, L. D.
- Venue
- Nature Biotechnology
- Published
- 2019-08-19
- Volume
- 37
- Issue
- 10
- Pages
- 1186-1197
- ISSN
- 0733-222X (ISSN-L)
- 1087-0156
- 1546-1696
- OpenAlex
- W2967078590
- Cited by
- 297
- References
- 3
- FWCI
- 21.62
- Type
- journal article
- Language
- en
- Open access
- green
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- Mourtada, R., Herce, H. D., Yin, D. J., Moroco, J. A., Wales, T. E., Engen, J. R., & Walensky, L. D. (2019). Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice. Nature Biotechnology. https://doi.org/10.1038/s41587-019-0222-z
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