ArticleJournal of functional biomaterials2024
Effect of Surface-Immobilized States of Antimicrobial Peptides on Their Ability to Disrupt Bacterial Cell Membrane Structure.
Article in Journal of functional biomaterials, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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.
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Who cites it
5 citing papers in PubMed.
- Antimicrobial Peptides in Preventive Medicine: Current Perspectives on Coating Strategies.ACS infectious diseases · 2026Review
- Covalently Immobilized Mitomycin C on Polypropylene Sutures Creates a Non-Releasing Bioactive Interface That Modulates Vascular Smooth Muscle Cell Fate and Prevents Intimal Hyperplasia.International journal of molecular sciences · 2026Article
- Machine learning-driven discovery of antimicrobial peptides againstFrontiers in pharmacology · 2026Article
- Cold Shock-Induced Nanocomposite Polymer Packaging Maintains Postharvest Quality of Vegetable Soybeans.Foods (Basel, Switzerland) · 2025Article
- Protein-based nanoparticles for antimicrobial and cancer therapy: implications for public health.RSC advances · 2025Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Antimicrobial peptide (AMP) surfaces are widely used to inhibit biofilm formation and bacterial infection. However, endpoint-immobilized AMPs on surfaces are totally different from free-state AMPs due to the constraints of the surface. In this work, the interactions between AMPs and bacterial cell membranes were analyzed through coarse-grained molecular dynamics and all-atom molecular dynamics simulations. This AMP disrupted membrane structure by altering the thickness and curvature of the membrane. Furthermore, the effect of surface-immobilized states of AMPs on their ability to disrupt membrane structure was revealed. The immobilized AMPs in the freeze-N system could bind to the membrane and disrupt the membrane structure through electrostatic forces between positively charged N-terminal amino acid residues and the negatively charged membrane, while the immobilized AMPs in the freeze-C system were repelled. The results will aid in the rational design of new AMP surfaces with enhanced efficacy and stability.
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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.