ArticleThe Journal of biological chemistry2019
Structural insights into the combinatorial effects of antimicrobial peptides reveal a role of aromatic-aromatic interactions in antibacterial synergism.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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Who cites it
17 citing papers in PubMed.
- Transgenic Tobacco Plants Expressing Synthetic Peptides: A Functional and Structural Analysis for Pathogen Resistance.Plant biotechnology journal · 2026Article
- Structures, Interactions, and Antimicrobial Activity of the Shortest Thanatin Peptide fromInternational journal of molecular sciences · 2025Article
- Innovative vibriosis control in open aquaculture: Paratapes undulata as a sustainable growth and resistance enhancer in red tilapia.Scientific reports · 2025Article
- Identification ofBiomolecules · 2025Article
- Single Disulfide Bond in Host Defense Thanatin Analog Peptides: Antimicrobial Activity, Atomic-Resolution Structures and Target Interactions.International journal of molecular sciences · 2024Article
- LL-37: Structures, Antimicrobial Activity, and Influence on Amyloid-Related Diseases.Biomolecules · 2024Review
- Hybrid 2D/3D-quantitative structure-activity relationship studies on the bioactivities and molecular mechanism of antibacterial peptides.Amino acids · 2024Article
- Outer-Membrane Permeabilization, LPS Transport Inhibition: Activity, Interactions, and Structures of Thanatin Derived Antimicrobial Peptides.International journal of molecular sciences · 2024Article
- Design and evaluation of tadpole-like conformational antimicrobial peptides.Communications biology · 2023Article
- Antimicrobial Peptides in Infectious Diseases and Beyond-A Narrative Review.Life (Basel, Switzerland) · 2023Review
- A rationally designed synthetic antimicrobial peptide against Pseudomonas-associated corneal keratitis: Structure-function correlation.Biophysical chemistry · 2022Article
- Atomic-Resolution Structures and Mode of Action of Clinically Relevant Antimicrobial Peptides.International journal of molecular sciences · 2022Review
- Advances and perspectives for antimicrobial peptide and combinatory therapies.Frontiers in bioengineering and biotechnology · 2022Review
- Evaluation of Three Antimicrobial Peptides Mixtures to Control the Phytopathogen Responsible for Fire Blight Disease.Plants (Basel, Switzerland) · 2021Article
- Antimicrobial peptides: mechanism of action, activity and clinical potential.Military Medical Research · 2021Review
- Thanatin: An Emerging Host Defense Antimicrobial Peptide with Multiple Modes of Action.International journal of molecular sciences · 2021Review
- Design, Engineering and Discovery of Novel α-Helical and β-Boomerang Antimicrobial Peptides against Drug Resistant Bacteria.International journal of molecular sciences · 2020Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The recent development of plants that overexpress antimicrobial peptides (AMPs) provides opportunities for controlling plant diseases. Because plants employ a broad-spectrum antimicrobial defense, including those based on AMPs, transgenic modification for AMP overexpression represents a potential way to utilize a defense system already present in plants. Herein, using an array of techniques and approaches, we report on VG16KRKP and KYE28, two antimicrobial peptides, which in combination exhibit synergistic antimicrobial effects against plant pathogens and are resistant against plant proteases. Investigating the structural origin of these synergistic antimicrobial effects with NMR spectroscopy of the complex formed between these two peptides and their mutated analogs, we demonstrate the formation of an unusual peptide complex, characterized by the formation of a bulky hydrophobic hub, stabilized by aromatic zippers. Using three-dimensional structure analyses of the complex in bacterial outer and inner membrane components and when bound to lipopolysaccharide (LPS) or bacterial membrane mimics, we found that this structure is key for elevating antimicrobial potency of the peptide combination. We conclude that the synergistic antimicrobial effects of VG16KRKP and KYE28 arise from the formation of a well-defined amphiphilic dimer in the presence of LPS and also in the cytoplasmic bacterial membrane environment. Together, these findings highlight a new application of solution NMR spectroscopy to solve complex structures to study peptide-peptide interactions, and they underscore the importance of structural insights for elucidating the antimicrobial effects of AMP mixtures.
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