ArticleNature communications2018
X-ray structure of a carpet-like antimicrobial defensin-phospholipid membrane disruption complex.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 69 citations in OpenAlex.
- Peptide-Based Delivery Systems: Selected Insights into Cell-Penetrating Peptides.ACS chemical neuroscience · 2026Review
- Mechanistic Insights into Human Defensin Antimicrobial Activity from Membrane Simulations.The Journal of membrane biology · 2026Article
- Advances in antimicrobial peptides: promising cancer treatments and vaccines.Frontiers in medicine · 2026Review
- Defensins as natural antimicrobial peptide scaffolds against antimicrobial-resistant pathogens: mechanisms, resistance risks, and translational prospects.Frontiers in cellular and infection microbiology · 2026Review
- Antimicrobial peptides in the era of resistance: integrating AI-driven design, host-microbe interactions, and nanotechnological delivery.Frontiers in microbiology · 2026Review
- Anticandidal Activity and Low Cytotoxicity of Modified Analogues of the Tobacco Defensin NaD1.Antibiotics (Basel, Switzerland) · 2025Article
- The Influence of POPC as a Coaggregate in Amyloid-β Oligomer Formation.ACS chemical neuroscience · 2025Article
- Production, Delivery, and Regulatory Aspects for Application of Plant-Based Anti-microbial Peptides: a Comprehensive Review.Probiotics and antimicrobial proteins · 2025Review
- Synthesis and Evaluation of Aquatic Antimicrobial Peptides Derived from Marine Metagenomes Using a High-Throughput Screening Approach.Marine drugs · 2025Article
- Expression of a novel NaD1 recombinant antimicrobial peptide enhances antifungal and insecticidal activities.Scientific reports · 2024Article
- The Plant Defensin Ppdef1 Is a Novel Topical Treatment for Onychomycosis.Journal of fungi (Basel, Switzerland) · 2023Article
- Defensin-based therapeutic peptide design in attenuating V30M TTR-induced Familial Amyloid Polyneuropathy.3 Biotech · 2023Article
- Anti-Cancer Peptides: Status and Future Prospects.Molecules (Basel, Switzerland) · 2023Review
- The cyclic peptide G4CP2 enables the modulation of galactose metabolism in yeast by interfering with GAL4 transcriptional activity.Frontiers in molecular biosciences · 2023Article
- Specific Lipid Studies in Complex Membranes by Solid-State NMR Spectroscopy.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- The potential of plant proteins as antifungal agents for agricultural applications.Synthetic and systems biotechnology · 2022Review
- Amyloidogenic Peptides: New Class of Antimicrobial Peptides with the Novel Mechanism of Activity.International journal of molecular sciences · 2022Review
- Polymeric Coatings and Antimicrobial Peptides as Efficient Systems for Treating Implantable Medical Devices Associated-Infections.Polymers · 2022Review
- Defensin-lipid interactions in membrane targeting: mechanisms of action and opportunities for the development of antimicrobial and anticancer therapeutics.Biochemical Society transactions · 2022Review
- Natural Peptides Inducing Cancer Cell Death: Mechanisms and Properties of Specific Candidates for Cancer Therapeutics.Molecules (Basel, Switzerland) · 2021Review
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Defensins are cationic antimicrobial peptides expressed throughout the plant and animal kingdoms as a first line of defense against pathogens. Membrane targeting and disruption is a crucial function of many defensins, however the precise mechanism remains unclear. Certain plant defensins form dimers that specifically bind the membrane phospholipids phosphatidic acid (PA) and phosphatidylinositol 4,5-bisphosphate, thereby triggering the assembly of defensin-lipid oligomers that permeabilize cell membranes. To understand this permeabilization mechanism, here we determine the crystal structure of the plant defensin NaD1 bound to PA. The structure reveals a 20-mer that adopts a concave sheet- or carpet-like topology where NaD1 dimers form one face and PA acyl chains form the other face of the sheet. Furthermore, we show that Arg39 is critical for PA binding, oligomerization and fungal cell killing. These findings identify a putative defensin-phospholipid membrane attack configuration that supports a longstanding proposed carpet mode of membrane disruption.
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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.