ArticleJournal of medicinal chemistry2022
Site-Specific Isopeptide Bond Formation: A Powerful Tool for the Generation of Potent and Nontoxic Antimicrobial Peptides.
Article in Journal of medicinal chemistry, 2022. 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.
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
9 citing papers in PubMed.
- Modulating Antimicrobial Activity and Structure of the Peptide Esc(1-21) via Site-Specific Isopeptide Bond Formation.Journal of peptide science : an official publication of the European Peptide Society · 2025Article
- Effect of Poly-γ-Glutamic Acid Molecular Weight on the Properties of Whey Protein Isolate Hydrogels.Polymers · 2025Article
- Engineering a Fusion Protein Biomaterial Based on SpyTag/SpyCatcher Bioconjugation of Elastin and Collagen Synthetic Proteins.ACS omega · 2025Article
- The Role and Mechanisms of Antimicrobial Peptides in Overcoming Multidrug-Resistant Bacteria.Molecules (Basel, Switzerland) · 2024Review
- Development of Nontoxic Peptides for Lipopolysaccharide Neutralization and Sepsis Treatment.ACS pharmacology & translational science · 2024Article
- To Fold or Not to Fold: Diastereomeric Optimization of an α-Helical Antimicrobial Peptide.Journal of medicinal chemistry · 2023Article
- Truncated Pleurocidin Derivative with High Pepsin Hydrolysis Resistance to Combat Multidrug-Resistant Pathogens.Pharmaceutics · 2022Article
- Designed Multifunctional Peptides for Intracellular Targets.Antibiotics (Basel, Switzerland) · 2022Review
- Hydrophobic-hydrophilic Alternation: An effective Pattern to de novo Designed Antimicrobial Peptides.Current pharmaceutical design · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antimicrobial peptides (AMPs) have the potential to treat multidrug-resistant bacterial infections. However, the clinical application of AMPs is prevented by their toxicity and poor proteolytic stability. Here, a site-specific approach is used to generate new AMPs to improve their efficacy against bacterial pathogens while reducing their toxicity. We modified and generated a new series of antimicrobial peptides from the leucine- and lysine-rich antimicrobial peptide Amp1L (LKLLKKLLKKLLKLL) by the site-specific incorporation of an isopeptide bond while retaining the peptide's size, sequence, charge, and molecular weight. This single bond switch provides the peptides with a weak helical conformation, strong antimicrobial activity, resistance to proteolytic degradation, low toxicity, and lower hemolytic activity. This new site-specific approach offers a powerful tool for developing potent and nontoxic antimicrobial drugs.
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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.