ArticleProceedings of the National Academy of Sciences of the United States of America2015
Helical antimicrobial polypeptides with radial amphiphilicity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
58 citing papers in PubMed, 220 citations in OpenAlex.
- Article
- Combating Antimicrobial Resistance with Hydrophilic and Eco-Friendly Membrane-Active Antibiotics Derived from Biological Nanoparticles.ACS nanoscience Au · 2026Article
- Self-adjuvanting α-helical polypeptide simultaneously delivers neoantigen mRNAs and activates dendritic cells to eradicate tumors.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Potent Racemic Antimicrobial Polypeptides Uncovered by a Stereochemical Series of Cationic d/l Backbones.Journal of the American Chemical Society · 2026Article
- Effective combinatorial antifungal therapy using a host defense peptide mimic that self-assembles into delivery micelles.Nature biotechnology · 2026Article
- A biodegradable antimicrobial oligomer-containing hydrogel for drug-resistant bacteria-infected skin wound treatment.Pharmaceutical science advances · 2025Article
- An antimicrobial peptide as a potential therapy for bacterial pneumonia that alleviates antimicrobial resistance.Nature communications · 2025Article
- Biosourced Functional Hydroxybenzoate-Journal of the American Chemical Society · 2025Article
- The Role of Flexibility in the Bioactivity of Short α-Helical Antimicrobial Peptides.Antibiotics (Basel, Switzerland) · 2025Review
- A plant peptide with dual activity against multidrug-resistant bacterial and fungal pathogens.Science advances · 2025Article
- The role of secondary structures of peptide polymers on antimicrobial efficacy and antibiotic potentiation.bioRxiv : the preprint server for biology · 2024Article
- Structure-Guided Bacteria Specificity and Wide Activity Spectrum of Endotoxin-Responsive Peptide Nanonets.Nano letters · 2024Article
- Helicity-directed recognition of bacterial phospholipid via radially amphiphilic antimicrobial peptides.Science advances · 2024Article
- AI-guided few-shot inverse design of HDP-mimicking polymers against drug-resistant bacteria.Nature communications · 2024Article
- A dual-targeting antifungal is effective against multidrug-resistant human fungal pathogens.Nature microbiology · 2024Article
- Inhaled immunoantimicrobials for the treatment of chronic obstructive pulmonary disease.Science advances · 2024Article
- Article
- Recent developments in membrane targeting antifungal agents to mitigate antifungal resistance.RSC medicinal chemistry · 2023Review
- Switching from membrane disrupting to membrane crossing, an effective strategy in designing antibacterial polypeptide.Science advances · 2023Article
- pH-activated antibiofilm strategies for controlling dental caries.Frontiers in cellular and infection microbiology · 2023Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
α-Helical antimicrobial peptides (AMPs) generally have facially amphiphilic structures that may lead to undesired peptide interactions with blood proteins and self-aggregation due to exposed hydrophobic surfaces. Here we report the design of a class of cationic, helical homo-polypeptide antimicrobials with a hydrophobic internal helical core and a charged exterior shell, possessing unprecedented radial amphiphilicity. The radially amphiphilic structure enables the polypeptide to bind effectively to the negatively charged bacterial surface and exhibit high antimicrobial activity against both gram-positive and gram-negative bacteria. Moreover, the shielding of the hydrophobic core by the charged exterior shell decreases nonspecific interactions with eukaryotic cells, as evidenced by low hemolytic activity, and protects the polypeptide backbone from proteolytic degradation. The radially amphiphilic polypeptides can also be used as effective adjuvants, allowing improved permeation of commercial antibiotics in bacteria and enhanced antimicrobial activity by one to two orders of magnitude. Designing AMPs bearing this unprecedented, unique radially amphiphilic structure represents an alternative direction of AMP development; radially amphiphilic polypeptides may become a general platform for developing AMPs to treat drug-resistant bacteria.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.