ArticleThe Journal of biological chemistry2013
Anti-antimicrobial peptides: folding-mediated host defense antagonists.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Probing theRSC chemical biology · 2026Article
- Unraveling lipid and inflammation interplay in cancer, aging and infection for novel theranostic approaches.Frontiers in immunology · 2024Review
- Anticancer activities of natural antimicrobial peptides from animals.Frontiers in microbiology · 2023Review
- SuPepMem: A database of innate immune system peptides and their cell membrane interactions.Computational and structural biotechnology journal · 2022Article
- Switching Cytolytic Nanopores into Antimicrobial Fractal Ruptures by a Single Side Chain Mutation.ACS nano · 2021Article
- Activated Polyhydroxyalkanoate Meshes Prevent Bacterial Adhesion and Biofilm Development in Regenerative Medicine Applications.Frontiers in bioengineering and biotechnology · 2020Article
- Delving Into the Origin of Destructive Inflammation in COVID-19: A Betrayal of Natural Host Defense Peptides?Frontiers in immunology · 2020Article
- A microfluidic platform for the characterisation of membrane active antimicrobials.Lab on a chip · 2019Article
- Tuneable poration: host defense peptides as sequence probes for antimicrobial mechanisms.Scientific reports · 2018Article
- Antimicrobial peptide capsids of de novo design.Nature communications · 2017Article
- Engineering monolayer poration for rapid exfoliation of microbial membranes.Chemical science · 2017Article
- Potent Inducers of Endogenous Antimicrobial Peptides for Host Directed Therapy of Infections.Scientific reports · 2016Article
- Autonomously folded α-helical lockers promote RNAi.Scientific reports · 2016Article
- Antimicrobial peptides.Pharmaceuticals (Basel, Switzerland) · 2013Article
Corrections and comments
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Authors and funding
14 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antimicrobial or host defense peptides are innate immune regulators found in all multicellular organisms. Many of them fold into membrane-bound α-helices and function by causing cell wall disruption in microorganisms. Herein we probe the possibility and functional implications of antimicrobial antagonism mediated by complementary coiled-coil interactions between antimicrobial peptides and de novo designed antagonists: anti-antimicrobial peptides. Using sequences from native helical families such as cathelicidins, cecropins, and magainins we demonstrate that designed antagonists can co-fold with antimicrobial peptides into functionally inert helical oligomers. The properties and function of the resulting assemblies were studied in solution, membrane environments, and in bacterial culture by a combination of chiroptical and solid-state NMR spectroscopies, microscopy, bioassays, and molecular dynamics simulations. The findings offer a molecular rationale for anti-antimicrobial responses with potential implications for antimicrobial resistance.
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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.