The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Helical Peptoid Mimics of Magainin-2 Amide
Abstract
A series of peptoid oligomers were designed as helical, cationic, and facially amphipathic mimics of the magainin-2 amide antibacterial peptide. We used circular dichroism spectroscopy to determine the conformation of these peptoids in aqueous buffer and in the presence of bacterial membrane-mimetic lipid vesicles, composed of a 7:3 mol ratio of POPE:POPG. We found that certain peptoids, which displayed characteristically helical CD in buffer and lipid vesicles, exhibit selective (nonhemolytic) and potent antibacterial activity against both Gram-positive and Gram-negative bacteria. In contrast, peptoids that exhibit weak CD, reminiscent of that of a peptide random coil, were ineffective antibiotics. In a manner similar to the natural magainin peptides, we find a correlation between peptoid lipophilicity and hemolytic propensity. We observe that a minimum length of approximately 12 peptoid residues may be required for antibacterial activity. We also see evidence that a helix length between 24 and 34 A may provide optimal antibacterial efficacy. These results provide the first example of a water-soluble, structured, bioactive peptoid.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Gellman, S. H. (1998) · Accounts of Chemical Research · doi:10.1021/ar960298r · Cited by 2,506
Zuckermann, R. N., Kerr, J. M., Kent, S. B. H., & Moos, W. H. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00052a076 · Cited by 1,277
Non-haemolytic β-amino-acid oligomers
Porter, E. A., Wang, X., Lee, H.-S., Weisblum, B., & Gellman, S. H. (2000) · Nature · doi:10.1038/35007145 · Cited by 671
Structure and Functions of Channel-Forming Peptides: Magainins, Cecropins, Melittin and Alamethicin
Bechinger, B. (1997) · Journal of Membrane Biology · doi:10.1007/s002329900201 · Cited by 602
Miller, S. M., Simon, R. J., Ng, S., Zuckermann, R. N., Kerr, J. M., & Moos, W. H. (1995) · Drug Development Research · doi:10.1002/ddr.430350105 · Cited by 429
Mimicry of Host-Defense Peptides by Unnatural Oligomers: Antimicrobial β-Peptides
Porter, E. A., Weisblum, B., & Gellman, S. H. (2002) · Journal of the American Chemical Society · doi:10.1021/ja0260871 · Cited by 379
Antimicrobial activity of synthetic magainin peptides and several analogues.
Zasloff, M., Martin, B., & Chen, H. C. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.3.910 · Cited by 373
Mimicry of bioactive peptides via non-natural, sequence-specific peptidomimetic oligomers
Patch, J. A., & Barron, A. E. (2002) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(02)00385-x · Cited by 255
Self-citationBioinspired polymeric materials: in-between proteins and plastics
Barron, A. E., & Zuckerman, R. N. (1999) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)00026-5 · Cited by 186
Self-citationSanborn, T. J., Wu, C. W., Zuckermann, R. N., & Barron, A. E. (2002) · Biopolymers · doi:10.1002/bip.1058 · Cited by 158
Self-citation
Cited by
Dill, K. A., Ozkan, S. B., Shell, M. S., & Weikl, T. R. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.092707.153558 · Cited by 1,163
Cationic Antimicrobial Polymers and Their Assemblies
Carmona-Ribeiro, A., & De Melo Carrasco, L. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14059906 · Cited by 532
Coarse grain models and the computer simulation of soft materials
Nielsen, S. O., Lopez, C. F., Srinivas, G., & Klein, M. L. (2004) · Journal of Physics: Condensed Matter · doi:10.1088/0953-8984/16/15/r03 · Cited by 423
Kuroda, K., Caputo, G. A., & DeGrado, W. F. (2009) · Chemistry – A European Journal · doi:10.1002/chem.200801523 · Cited by 346
γ-AApeptides as a New Strategy for Therapeutic Development
Nimmagadda, A., Shi, Y., & Cai, J. (2019) · Current Medicinal Chemistry · doi:10.2174/0929867324666171107095913 · Cited by 21
Metadata
- Authors
- Patch, J. A., & Barron, A. E.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2003-09-16
- Volume
- 125
- Issue
- 40
- Pages
- 12092-12093
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2050140989
- Cited by
- 375
- References
- 10
- FWCI
- 11.89
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
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).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
