ArticleACS infectious diseases2021
Switching Bond: Generation of New Antimicrobial Peptides via the Incorporation of an Intramolecular Isopeptide Bond.
Article in ACS infectious diseases, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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.
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
9 citing papers in PubMed, 18 citations in OpenAlex.
- Engineering Antimicrobial Peptides via Motif Assembly for Combating Multidrug-Resistant Pathogens.Journal of medicinal chemistry · 2026Article
- 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
- The effect of C-terminal deamidation on bacterial susceptibility and resistance to modelin-5.European biophysics journal : EBJ · 2025Article
- Development of Nontoxic Peptides for Lipopolysaccharide Neutralization and Sepsis Treatment.ACS pharmacology & translational science · 2024Article
- Exploring the Potential of Isalo Scorpion Cytotoxic Peptide in Enhancing Gill Barrier Function and Immunity in Grass Carp (Aquaculture nutrition · 2024Article
- Interaction of Pexiganan (MSI-78)-Derived Analogues Reduces Inflammation and TLR4-Mediated Cytokine Secretion: A Comparative Study.ACS omega · 2023Article
- Antimicrobial Peptides against Multidrug-ResistantJournal of medicinal chemistry · 2022Article
- Site-Specific Isopeptide Bond Formation: A Powerful Tool for the Generation of Potent and Nontoxic Antimicrobial Peptides.Journal of medicinal chemistry · 2022Article
- Hydrophobic-hydrophilic Alternation: An effective Pattern to de novo Designed Antimicrobial Peptides.Current pharmaceutical design · 2022Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antimicrobial peptides (AMPs), which can be modified to kill a broad spectrum of microoganisms or a specific microorganism, are considered as promising alternatives to combat the rapidly widespread, resistant bacterial infections. However, there are still several obstacles to overcome. These include toxicity, stability, and the ability to interfere with the immune response and bacterial resistance. To overcome these challenges, we herein replaced the regular peptide bonds with isopeptide bonds to produce new AMPs based on the well-known synthetic peptides Amp1L and MSI-78 (pexiganan). Two new peptides Amp1EP and MSIEP were generated while retaining properties such as size, sequence, charge, and molecular weight. These new peptides have reduced toxicity toward murine macrophage (RAW 264.7) cells, human monocytic (THP-1) cells, and human red blood cells (hRBCs) and enhanced the stability toward proteolytic degradation. Importantly, the new peptides do not repress the pro-inflammatory cytokine and hence should not modulate the immune response. Structurally, the new peptides, Amp1EP and MSIEP, have a structure of random coils in contrast to the helical structures of the parental peptides as revealed by circular dichroism (CD) analysis. Their mode of action, assessed by flow cytometry, includes permeabilization of the bacterial membrane. Overall, we present here a new approach to modulate AMPs to develop antimicrobial peptides for future therapeutic purposes.
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Registered trials
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