ArticleEuropean biophysics journal : EBJ2011
A kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments.
Article in European biophysics journal : EBJ, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 23 citations in OpenAlex.
- Three Decades of REDOR in Protein Science: A Solid-State NMR Technique for Distance Measurement and Spectral Editing.International journal of molecular sciences · 2023Review
- Conformation and membrane interaction studies of the potent antimicrobial and anticancer peptide palustrin-Ca.Scientific reports · 2021Article
- Bioinformatic Analysis of 1000 Amphibian Antimicrobial Peptides Uncovers Multiple Length-Dependent Correlations for Peptide Design and Prediction.Antibiotics (Basel, Switzerland) · 2020Article
- Review
- NMR model structure of the antimicrobial peptide maximin 3.European biophysics journal : EBJ · 2019Article
- Modular toxin from the lynx spider Oxyopes takobius: Structure of spiderine domains in solution and membrane-mimicking environment.Protein science : a publication of the Protein Society · 2017Article
- Potential Use of Antimicrobial Peptides as Vaginal Spermicides/Microbicides.Pharmaceuticals (Basel, Switzerland) · 2016Review
- Modeling Protein-Micelle Systems in Implicit Water.The journal of physical chemistry. B · 2015Article
- High-resolution structures and orientations of antimicrobial peptides piscidin 1 and piscidin 3 in fluid bilayers reveal tilting, kinking, and bilayer immersion.Journal of the American Chemical Society · 2014Article
- Novel method to identify the optimal antimicrobial peptide in a combination matrix, using anoplin as an example.Antimicrobial agents and chemotherapy · 2014Article
- A kinked antimicrobial peptide from Bombina maxima. II. Behavior in phospholipid bilayers.European biophysics journal : EBJ · 2011Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Maximin-4 is a 27-residue cationic antimicrobial peptide exhibiting selectivity for bacterial cells. As part of the innate defense system in the Chinese red-belly toad, its mode of action is thought to be ion channel or pore formation and dissipation of the electrochemical gradient across the pathogenic cell membrane. Here we present the high-resolution structure of maximin-4 in two different membrane mimetics, sodium dodecyl sulfate micelles and 50% methanol, as determined by (1)H solution NMR spectroscopy. In both environments, the peptide chain adopts a helix-break-helix conformation following a highly disordered N-terminal segment. Despite the similarities in the overall topology of the two structures, major differences are observed in terms of the interactions stabilizing the kink region and the arrangement of the four lysine residues. This has a marked influence on the shape and charge distribution of the molecule and may have implications for the bacterial selectivity of the peptide. The solution NMR results are complemented by CD spectroscopy and solid-state NMR experiments in lipid bilayers, both confirming the predominantly helical conformation of the peptide. As a first step in elucidating the membrane interactions of maximin-4, our study contributes to a better understanding of the mode of action of antimicrobial peptides and the factors governing their selectivity.
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