ArticleInternational journal of molecular sciences2020
Antimicrobial Peptides with Enhanced Salt Resistance and Antiendotoxin Properties.
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 20 citations in OpenAlex.
- In silico design and In Vitro validation of WK15: a promising antimicrobial peptide for aquaculture applications.World journal of microbiology & biotechnology · 2026Article
- Differential antimicrobial activity of two LL37 derivatives against periodontal bacteria, including enhanced efficacy againstFrontiers in microbiology · 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
- Sequence Permutation Generated Lysine and Tryptophan-Rich Antimicrobial Peptides with Enhanced Therapeutic Index.Antibiotics (Basel, Switzerland) · 2025Article
- Production, Delivery, and Regulatory Aspects for Application of Plant-Based Anti-microbial Peptides: a Comprehensive Review.Probiotics and antimicrobial proteins · 2025Review
- Antimicrobial Peptides: A Promising Alternative to Conventional Antimicrobials for Combating Polymicrobial Biofilms.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Improved Antimicrobial Activity of Bovine Lactoferrin Peptide (LFcinB) Based on Rational Design.The protein journal · 2023Article
- Article
- The antimicrobial peptide database is 20 years old: Recent developments and future directions.Protein science : a publication of the Protein Society · 2023Article
- Antimicrobial Peptides and Cell-Penetrating Peptides: Non-Antibiotic Membrane-Targeting Strategies Against Bacterial Infections.Infection and drug resistance · 2023Review
- High Level Expression and Purification of Cecropin-like Antimicrobial Peptides inBiomedicines · 2022Article
- A Multiplexed Cell-Free Assay to Screen for Antimicrobial Peptides in Double Emulsion Droplets.Angewandte Chemie (International ed. in English) · 2022Article
- Isolation of the mustard Napin proteinBiochemistry and biophysics reports · 2022Article
- Florfenicol-Polyarginine Conjugates Exhibit Promising Antibacterial Activity Against Resistant Strains.Frontiers in chemistry · 2022Article
- Thanatin: An Emerging Host Defense Antimicrobial Peptide with Multiple Modes of Action.International journal of molecular sciences · 2021Review
- Boosting Synergistic Effects of Short Antimicrobial Peptides With Conventional Antibiotics Against Resistant Bacteria.Frontiers in microbiology · 2021Article
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 2 institutions in 2 countries.
Funding
Abstract
A strategy was described to design antimicrobial peptides (AMPs) with enhanced salt resistance and antiendotoxin activities by linking two helical AMPs with the Ala-Gly-Pro (AGP) hinge. Among the designed peptides, KR12AGPWR6 demonstrated the best antimicrobial activities even in high salt conditions (NaCl ~300 mM) and possessed the strongest antiendotoxin activities. These activities may be related to hydrophobicity, membrane-permeability, and α-helical content of the peptide. Amino acids of the C-terminal helices were found to affect the peptide-induced permeabilization of LUVs, the α-helicity of the designed peptides under various LUVs, and the LPS aggregation and size alternation. A possible model was proposed to explain the mechanism of LPS neutralization by the designed peptides. These findings could provide a new approach for designing AMPs with enhanced salt resistance and antiendotoxin activities for potential therapeutic applications.
Indexed as
Identifiers
What OpenQuestion holds
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.