ArticleBiophysical journal2016
Structural and Dynamic Insights of the Interaction between Tritrpticin and Micelles: An NMR Study.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Antimicrobial peptides: from discovery to developmental applications.Applied and environmental microbiology · 2025Review
- Antibiofilm Activities of Tritrpticin Analogs Against PathogenicMolecules (Basel, Switzerland) · 2025Article
- Molecular Interactions of the Antimicrobial Peptide Tritrpticin with Mixed Nanoaggregates: A Fluorescence Spectroscopy Study.Protein and peptide letters · 2025Article
- Single-Micelle and Single-Zinc-Particle Imaging Provides Insights into the Physical Processes Underpinning Organozinc Reactions in Water.Journal of the American Chemical Society · 2022Article
- Insights Into the Micelle-Induced β-Hairpin-to-α-Helix Transition of a LytA-Derived Peptide by Photo-CIDNP Spectroscopy.International journal of molecular sciences · 2021Article
- Review
- A Dynamic Overview of Antimicrobial Peptides and Their Complexes.Molecules (Basel, Switzerland) · 2018Review
- Article
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Authors and funding
6 authors.
Funding
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Abstract
A large number of antimicrobial peptides (AMPs) acts with high selectivity and specificity through interactions with membrane lipid components. These peptides undergo complex conformational changes in solution; upon binding to an interface, one major conformation is stabilized. Here we describe a study of the interaction between tritrpticin (TRP3), a cathelicidin AMP, and micelles of different chemical composition. The peptide's structure and dynamics were examined using one-dimensional and two-dimensional NMR. Our data showed that the interaction occurred by conformational selection and the peptide acquired similar structures in all systems studied, despite differences in detergent headgroup charge or dipole orientation. Fluorescence and paramagnetic relaxation enhancement experiments showed that the peptide is located in the interface region and is slightly more deeply inserted in 1-myristoyl-2-hydroxy-sn-glycero-3-phospho-1'-rac-glycerol (LMPG, anionic) than in 1-lauroyl-2-hydroxy-sn-glycero-3-phosphocholine (LLPC, zwitterionic) micelles. Moreover, the tilt angle of an assumed helical portion of the peptide is similar in both systems. In previous work we proposed that TRP3 acts by a toroidal pore mechanism. In view of the high hydrophobic core exposure, hydration, and curvature presented by micelles, the conformation of TRP3 in these systems could be related to the peptide's conformation in the toroidal pore.
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