The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Mimicry of Host-Defense Peptides by Unnatural Oligomers: Antimicrobial β-Peptides
Abstract
We have designed beta-amino acid oligomers that are helical, cationic, and amphiphilic with the intention of mimicking the biological activity of amphiphilic, cationic alpha-helical antimicrobial peptides found in nature (e.g., magainins). We have previously identified a 17-residue beta-peptide (called beta-17) with antibiotic activity similar to that of a magainin derivative against four bacterial species, including two clinical isolates that are resistant to common antibiotics. This beta-peptide displays very low hemolytic activity against human red blood cells, which indicates selectivity for bacterial cells over mammalian cells. Here we examine some of the factors important for activity in this class of beta-peptides. An amphiphilic helix is necessary, because a nonamphiphilic isomer proved to be inactive. The ratio of cationic to hydrophobic residues is also important. Active beta-peptides induce the leakage of beta-galactosidase from treated Bacillus subtilis cells, as do alpha-helical antibiotic peptides, and this similarity suggests that the beta-peptide mode of action involves disruption of microbial membranes. This class of beta-peptides is not degraded by proteases, which bodes well for biological applications.
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Cites
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Self-citationA spectrophotometric determination of trypsin and chymotrypsin
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Antibacterial peptides: basic facts and emerging concepts
Boman, H. G. (2003) · Journal of Internal Medicine · doi:10.1046/j.1365-2796.2003.01228.x · Cited by 1,158
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Peptoids that mimic the structure, function, and mechanism of helical antimicrobial peptides
Chongsiriwatana, N. P., Patch, J. A., Czyzewski, A. M., Dohm, M. T., Ivankin, A., Gidalevitz, D., Zuckermann, R. N., & Barron, A. E. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708254105 · Cited by 657
Combating Multidrug‐Resistant Bacteria: Current Strategies for the Discovery of Novel Antibacterials
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Helical Peptoid Mimics of Magainin-2 Amide
Patch, J. A., & Barron, A. E. (2003) · Journal of the American Chemical Society · doi:10.1021/ja037320d · Cited by 375
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Biomimetic antimicrobial polymers: recent advances in molecular design
Ergene, C., Yasuhara, K., & Palermo, E. F. (2018) · Polymer Chemistry · doi:10.1039/c8py00012c · Cited by 312
Spontaneous transmembrane pore formation by short-chain synthetic peptide
(2021) · doi:10.1016/j.bpj.2021.08.033 · Cited by 9
Metadata
- Authors
- Porter, E. A., Weisblum, B., & Gellman, S. H.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2002-06-01
- Volume
- 124
- Issue
- 25
- Pages
- 7324-7330
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W1975313075
- Cited by
- 379
- References
- 38
- FWCI
- 14.96
- Type
- journal article
- Language
- en
- Open access
- closed
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