ArticleAntimicrobial agents and chemotherapy2004
De novo design of potent antimicrobial peptides.
Article in Antimicrobial agents and chemotherapy, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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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.
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Who cites it
58 citing papers in PubMed, 154 citations in OpenAlex.
- Musical Peptide: Fragmentation of Musical Protein for AI-driven Bioactive Peptide Discovery Based on a New DeepPepQSAR Pipeline.Interdisciplinary sciences, computational life sciences · 2026Article
- DeepPepQSAR: all-in-one for comprehensively exploiting the vast molecular diversity space of bioactive peptide universe.Molecular diversity · 2026Article
- A Localization-Based Motif Combination Approach To the Design of Antimicrobial Peptides Targeting Gram-Positive and Gram-Negative Bacteria.Probiotics and antimicrobial proteins · 2026Article
- Human and Marine Host Defense Peptides for Healthy Skin.Marine drugs · 2026Review
- Deep learning in the discovery of antiviral peptides and peptidomimetics: databases and prediction tools.Molecular diversity · 2025Review
- Development of lysine-branched dendrimeric antimicrobial peptides targeting ESKAPE pathogens: broad-spectrum activity, biofilm eradication, and endotoxin neutralization.Frontiers in microbiology · 2025Article
- Dual Antibiotic Approach: Synthesis and Antibacterial Activity of Antibiotic-Antimicrobial Peptide Conjugates.Antibiotics (Basel, Switzerland) · 2024Review
- QSAR Reveals Decreased Lipophilicity of Polar Residues Determines the Selectivity of Antimicrobial Peptide Activity.ACS omega · 2024Article
- Cyclic Peptides in Pipeline: What Future for These Great Molecules?Pharmaceuticals (Basel, Switzerland) · 2023Review
- Rational design of hyperstable antibacterial peptides for food preservation.NPJ science of food · 2021Article
- The multifaceted nature of antimicrobial peptides: current synthetic chemistry approaches and future directions.Chemical Society reviews · 2021Review
- Molecular engineering of antimicrobial peptides: microbial targets, peptide motifs and translation opportunities.Biophysical reviews · 2021Review
- Polymyxins and Bacterial Membranes: A Review of Antibacterial Activity and Mechanisms of Resistance.Membranes · 2020Review
- An amphipathic peptide with antibiotic activity against multidrug-resistant Gram-negative bacteria.Nature communications · 2020Article
- Antimicrobial peptides: new hope in the war against multidrug resistance.Zoological research · 2019Review
- Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria.International journal of molecular sciences · 2019Article
- Computational prediction of plasma protein binding of cyclic peptides from small molecule experimental data using sparse modeling techniques.BMC bioinformatics · 2018Article
- Antibacterial Activity and Mechanism of Action of Bovine Lactoferricin Derivatives with Symmetrical Amino Acid Sequences.International journal of molecular sciences · 2018Article
- Antimicrobial resistance in livestock: antimicrobial peptides provide a new solution for a growing challenge.Animal frontiers : the review magazine of animal agriculture · 2018Article
- Designing Antibacterial Peptides with Enhanced Killing Kinetics.Frontiers in microbiology · 2018Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipopolysaccharide (LPS), shed by gram-negative bacteria during infection and antimicrobial therapy, may lead to lethal endotoxic shock syndrome. A rational design strategy based on the presumed mechanism of antibacterial effect was adopted to design cationic antimicrobial peptides capable of binding to LPS through tandemly repeated sequences of alternating cationic and nonpolar residues. The peptides were designed to achieve enhanced antimicrobial potency due to initial bacterial membrane binding with a reduced risk of endotoxic shock. The peptides designed displayed binding affinities to LPS and lipid A (LA) in the low micromolar range and by molecular modeling were predicted to form amphipathic beta-hairpin-like structures when they bind to LPS or LA. They also exhibited strong effects against gram-negative bacteria, with MICs in the nanomolar range, and low cytotoxic and hemolytic activities at concentrations significantly exceeding their MICs. Quantitative structure-activity relationship (QSAR) analysis of peptide sequences and their antimicrobial, cytotoxic, and hemolytic activities revealed that site-directed substitutions of residues in the hydrophobic face of the amphipathic peptides with less lipophilic residues selectively decrease the hemolytic effect without significantly affecting the antimicrobial or cytotoxic activity. On the other hand, the antimicrobial effect can be enhanced by substitutions in the polar face with more polar residues, which increase the amphipathicity of the peptide. On the basis of the QSARs, new analogs that have strong antimicrobial effects but that lack hemolytic activity can be proposed. The findings highlight the importance of peptide amphipathicity and allow a rational method that can be used to dissociate the antimicrobial and hemolytic effects of cationic peptides, which have potent antimicrobial properties, to be proposed.
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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.