ArticleFrontiers in microbiology2020
Systematically Studying the Optimal Amino Acid Distribution Patterns of the Amphiphilic Structure by Using the Ultrashort Amphiphiles.
Article in Frontiers in microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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.
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Who cites it
9 citing papers in PubMed, 28 citations in OpenAlex.
- Hybrid and conjugated antimicrobial peptides: new tactics to counter bacterial resistance.Frontiers in microbiology · 2026Review
- Unveiling the dual role ofPlant signaling & behavior · 2025Article
- Optimizing therapeutic efficacy of antifungal peptides via strategic terminal amino acid modification.Journal of advanced research · 2025Article
- Application of tobramycin benzyl ether as an antibiotic adjuvant capable of sensitizing multidrug-resistant Gram-negative bacteria to rifampicin.RSC medicinal chemistry · 2024Article
- Computational modelling of the antimicrobial peptides Cruzioseptin-4 extracted from the frog Cruziohyla calcarifer and Pictuseptin-1 extracted from the frog Boana picturata.Scientific reports · 2024Article
- Advancements in antimicrobial nanoscale materials and self-assembling systems.Chemical Society reviews · 2022Review
- Novel D-form of hybrid peptide (D-AP19) rapidly kills Acinetobacter baumannii while tolerating proteolytic enzymes.Scientific reports · 2022Article
- Hydrophobic-hydrophilic Alternation: An effective Pattern to de novo Designed Antimicrobial Peptides.Current pharmaceutical design · 2022Article
- Nanostructured Antimicrobial Peptides: Crucial Steps of Overcoming the Bottleneck for Clinics.Frontiers in microbiology · 2021Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amphipathicity has traditionally been considered to be essential for the de novo design or systematic optimization of antimicrobial peptides (AMPs). However, the current research methods to study the relationship between amphiphilicity and antimicrobial activity are inappropriate, because the key parameters (hydrophobicity, positive charge, etc.) and secondary structure of AMPs are changed. To systematically and accurately study the effects of amphiphilicity on antimicrobial properties of AMPs, we designed parallel series of AMPs with a different order of amino acids in a sequence composed only of Arg and either Trp (WR series) or Leu (LR series), under conditions in which other vital parameters were fixed. Furthermore, based on the WR and LR peptides that can form stable amphiphilic β-sheet structures in the anionic membrane-mimetic environment, we found that high β-sheet amphipathic was accompanied by strong antimicrobial activity. Of such peptides, W5 ([RW]
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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.