ArticleACS chemical biology2014
Transformation of human cathelicidin LL-37 into selective, stable, and potent antimicrobial compounds.
Article in ACS chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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
69 citing papers in PubMed, 1 synthesis or guideline pooled it, 116 citations in OpenAlex.
- Roles of d-Amino Acids on the Bioactivity of Host Defense Peptides.International journal of molecular sciences · 2016Pooled it
- Article
- Building Blocks of 2,3-Diaminopropionic Acid Functionalized with an Oxa-Acid Spacer Shift the Functional Profile of Human Cathelicidin LL-37: Enhanced Enzymatic Stability and Selective Suppression of Neutrophil Degranulation.Pharmaceuticals (Basel, Switzerland) · 2026Article
- Overcoming LPS-mediated resistance in gram-negative pathogens: a review of LL-37 analogs and computational design strategies.Archives of microbiology · 2026Review
- CAMPER: mechanistic artificial intelligence for designing peptides that target MRSA persisters.Nature communications · 2026Article
- Article
- One-Step Design of Potent and Nonhemolytic Antimicrobial Peptides by Using a Database-Guided, Nonmachine Learning Approach.ACS infectious diseases · 2026Article
- Impact of the Arrangement Modes of the Antimicrobial Motifs WWR-7 and its Analogs in CAMPs on Their Therapeutic Properties.Chemistry, an Asian journal · 2026Article
- BroadAMP-GPT: AI-Driven generation of broad-spectrum antimicrobial peptides for combating multidrug-resistant ESKAPE pathogens.Gut microbes · 2025Article
- NMR Unveils Activity Mechanism of Linear Spider Venom Peptide Fragments Selected by Neural Networks Against Staphylococci Including MRSA.Pharmaceutics · 2025Article
- Combating Fuel Biocontamination: Tailored Antimicrobial Peptides and an Innovative Delivery Strategy.ACS applied bio materials · 2025Article
- Antimicrobial Peptides of the Cathelicidin Family: Focus on LL-37 and Its Modifications.International journal of molecular sciences · 2025Review
- Segment-Based Peptide Design Reveals the Importance of N-Terminal High Cationicity for Antimicrobial Activity Against Gram-Negative Pathogens.Probiotics and antimicrobial proteins · 2025Article
- Preparation and characterization of immunopeptides isolated from pig spleen and evaluation of their immunomodulatory propertiesFrontiers in immunology · 2025Article
- Infective Endocarditis by Biofilm-Producing Methicillin-ResistantAntibiotics (Basel, Switzerland) · 2024Review
- Novel Tree Shrew-Derived Antimicrobial Peptide with Broad-Spectrum Antibacterial Activity.ACS omega · 2024Article
- Origami of KR-12 Designed Antimicrobial Peptides and Their Potential Applications.Antibiotics (Basel, Switzerland) · 2024Review
- Antimicrobial Properties and Cytotoxicity of LL-37-Derived Synthetic Peptides to Treat Orthopedic Infections.Antibiotics (Basel, Switzerland) · 2024Article
- Between good and evil: Complexation of the human cathelicidin LL-37 with nucleic acids.Biophysical journal · 2024Review
- Biofilm Producing Methicillin-ResistantPathogens (Basel, Switzerland) · 2024Review
9 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
This Letter reports a family of novel antimicrobial compounds obtained by combining peptide library screening with structure-based design. Library screening led to the identification of a human LL-37 peptide resistant to chymotrypsin. This d-amino-acid-containing peptide template was active against Escherichia coli but not methicillin-resistant Staphylococcus aureus (MRSA). It possesses a unique nonclassic amphipathic structure with hydrophobic defects. By repairing the hydrophobic defects, the peptide (17BIPHE2) gained activity against the ESKAPE pathogens, including Enterococcus faecium, S. aureus, Klebsiella pneumoniae, Acinetobacter baumanii, Pseudomonas aeruginosa, and Enterobacter species. In vitro, 17BIPHE2 could disrupt bacterial membranes and bind to DNA. In vivo, the peptide prevented staphylococcal biofilm formation in a mouse model of catheter-associated infection. Meanwhile, it boosted the innate immune response to further combat the infection. Because these peptides are potent, cell-selective, and stable to several proteases, they may be utilized to combat one or more ESKAPE pathogens.
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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.