ArticleThe Journal of biological chemistry2016
Role of Aromatic Amino Acids in Lipopolysaccharide and Membrane Interactions of Antimicrobial Peptides for Use in Plant Disease Control.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 49 citations in OpenAlex.
- Article
- Exploratory data analysis of physicochemical parameters of natural antimicrobial and anticancer peptides: Unraveling the patterns and trends for the rational design of novel peptides.BioImpacts : BI · 2024Article
- Potentiating Biosynthesis of Alkaloids and Polyphenolic Substances inMolecules (Basel, Switzerland) · 2023Article
- Integrated Transcriptome and Metabolome Analysis of Rice Leaves Response to High Saline-Alkali Stress.International journal of molecular sciences · 2023Article
- 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
- Probing the Functional Interaction Interface of Lipopolysaccharide and Antimicrobial Peptides: A Solution-State NMR Perspective.Methods in molecular biology (Clifton, N.J.) · 2022Article
- GeneFrontiers in microbiology · 2022Article
- Comparative Ionomics and Metabolic Responses and Adaptive Strategies of Cotton to Salt and Alkali Stress.Frontiers in plant science · 2022Article
- The Impact of Lung Proteases on Snake-Derived Antimicrobial Peptides.Biomolecules · 2021Article
- Novel antimicrobial peptide discovery using machine learning and biophysical selection of minimal bacteriocin domains.Drug development research · 2020Article
- Connections Between Amino Acid Metabolisms in Plants: Lysine as an Example.Frontiers in plant science · 2020Review
- Structural insights into the combinatorial effects of antimicrobial peptides reveal a role of aromatic-aromatic interactions in antibacterial synergism.The Journal of biological chemistry · 2019Article
- General lack of structural characterization of chemically synthesized long peptides.Protein science : a publication of the Protein Society · 2019Review
- The C-Terminal Domain of theToxins · 2019Article
- Article
- Structural basis for endotoxin neutralisation and anti-inflammatory activity of thrombin-derived C-terminal peptides.Nature communications · 2018Article
- Article
- Structural insights of a self-assembling 9-residue peptide from the C-terminal tail of the SARS corona virus E-protein in DPC and SDS micelles: A combined high and low resolution spectroscopic study.Biochimica et biophysica acta. Biomembranes · 2018Article
- Modification Targeting the "Rana Box" Motif of a Novel Nigrocin Peptide FromFrontiers in microbiology · 2018Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
KYE28 (KYEITTIHNLFRKLTHRLFRRNFGYT-LR), the representative sequence of helix D of heparin co-factor II, was demonstrated to be potent against agronomically important Gram-negative plant pathogens Xanthomonas vesicatoria and Xanthomonas oryzae, capable of inhibiting disease symptoms in detached tomato leaves. NMR studies in the presence of lipopolysaccharide provided structural insights into the mechanisms underlying this, notably in relationship to outer membrane permeabilization. The three-dimensional solution structure of KYE28 in LPS is characterized by an N-terminal helical segment, an intermediate loop followed by another short helical stretch, and an extended C terminus. The two termini are in close proximity to each other via aromatic packing interactions, whereas the positively charged residues form an exterior polar shell. To further demonstrate the importance of the aromatic residues for this, a mutant peptide KYE28A, with Ala substitutions at Phe(11), Phe(19), Phe(23), and Tyr(25) was designed, which showed attenuated antimicrobial activity at high salt concentrations, as well as lower membrane disruption and LPS binding abilities compared with KYE28. In contrast to KYE28, KYE28A adopted an extended helical structure in LPS with extended N and C termini. Aromatic packing interactions were completely lost, although hydrophobic interaction between the side chains of hydrophobic residues were still partly retained, imparting an amphipathic character and explaining its residual antimicrobial activity and LPS binding as observed from ellipsometry and isothermal titration calorimetry. We thus present key structural aspects of KYE28, constituting an aromatic zipper, of potential importance for the development of novel plant protection agents and therapeutic agents.
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