ArticleNanoscale2024
Emergent conformational and aggregation properties of synergistic antimicrobial peptide combinations.
Article in Nanoscale, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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
7 citing papers in PubMed.
- Sequence-Derived and Molecular Descriptors for Interpretable Modeling of Molecular Systems: Insights from Peptide Hemolysis.Journal of chemical information and modeling · 2026Article
- Aggregation-State Dynamics Drive Double Cooperativity Between Antimicrobial Peptides LL-37 and HNP1.Angewandte Chemie (International ed. in English) · 2026Article
- Predicting peptide orientation in membrane interactions: a review on transmembrane and surface-bound states.European biophysics journal : EBJ · 2026Review
- Mechanistic Disruption of the TREM2-DAP12 Transmembrane Complex by Alzheimer's Disease Mutations: A Multiscale Simulation Study.Journal of chemical information and modeling · 2025Article
- A Bioinspired Mastoparan Exhibits Concentration-Dependent Anti-Bacterial Activity via Membrane Disruption.ACS applied materials & interfaces · 2025Article
- Enhanced Gram-Negative Membrane Disruption and In Vivo Efficacy via Lysine-Arginine Enrichment of Opis16a.ACS medicinal chemistry letters · 2025Article
- Carboxy-Amidated AamAP1-Lys has Superior Conformational Flexibility and Accelerated Killing of Gram-Negative Bacteria.Biochemistry · 2025Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Synergy between antimicrobial peptides (AMPs) may be the key to their evolutionary success and could be exploited to develop more potent antibacterial agents. One of the factors thought to be essential for AMP potency is their conformational flexibility, but characterising the diverse conformational states of AMPs experimentally remains challenging. Here we introduce a method for characterising the conformational flexibility of AMPs and provide new insights into how the interplay between conformation and aggregation in synergistic AMP combinations yields emergent properties. We use unsupervised learning and molecular dynamics simulations to show that mixing two AMPs from the Winter Flounder family (pleurocidin (WF2) & WF1a) constrains their conformational space, reducing the number of distinct conformations adopted by the peptides, most notably for WF2. The aggregation behaviour of the peptides is also altered, favouring the formation of higher-order aggregates upon mixing. Critically, the interaction between WF1a and WF2 influences the distribution of WF2 conformations within aggregates, revealing how WF1a can modulate WF2 behaviour. Our work paves the way for deeper understanding of the synergy between AMPs, a fundamental process in nature.
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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 Socratic graph.