ArticleBiochimica et biophysica acta2011
Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR spectroscopy in zwitterionic and charged lipid bilayers.
Article in Biochimica et biophysica acta, 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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Who cites it
11 citing papers in PubMed, 31 citations in OpenAlex.
- Emergent conformational and aggregation properties of synergistic antimicrobial peptide combinations.Nanoscale · 2024Article
- Peptoid-based macrodiscs of variable lipid composition for structural studies of membrane proteins by oriented-sample solid-state NMR.Journal of structural biology: X · 2024Article
- Aligned peptoid-based macrodiscs for structural studies of membrane proteins by oriented-sample NMR.Biophysical journal · 2022Article
- Solid-State NMR of Membrane Proteins in Lipid Bilayers: To Spin or Not To Spin?Accounts of chemical research · 2021Review
- Revealing the Mechanisms of Synergistic Action of Two Magainin Antimicrobial Peptides.Frontiers in medical technology · 2020Review
- Protein Rotational Dynamics in Aligned Lipid Membranes Probed by Anisotropic TBiophysical journal · 2018Article
- Membrane interactions of phylloseptin-1, -2, and -3 peptides by oriented solid-state NMR spectroscopy.Biophysical journal · 2014Article
- Cobra cytotoxins: structural organization and antibacterial activity.Acta naturae · 2014Article
- On the role of NMR spectroscopy for characterization of antimicrobial peptides.Methods in molecular biology (Clifton, N.J.) · 2013Review
- Synthesis and characterization of the 47-residue heterodimeric antimicrobial peptide distinctin, featuring directed disulfide bridge formation.Biopolymers · 2012Article
- On the combined analysis of ²H and ¹⁵N/¹H solid-state NMR data for determination of transmembrane peptide orientation and dynamics.Biophysical journal · 2011Article
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
Abstract
Distinctin is a 47-residue antimicrobial peptide, which interacts with negatively charged membranes and is active against Gram-positive and Gram-negative bacteria. Its primary sequence comprises two linear chains of 22 (chain 1) and 25 (chain 2) residues, linked by a disulfide bridge between Cys19 of chain 1 and Cys23 of chain 2. Unlike other antimicrobial peptides, distinctin in the absence of the lipid membrane has a well-defined three-dimensional structure, which protects it from protease degradation. Here, we used static solid-state NMR spectroscopy in mechanically aligned lipid bilayers (charged or zwitterionic) to study the topology of distinctin in lipid bilayers. We found that this heterodimeric peptide adopts an ordered conformation absorbed on the surface of the membrane, with the long helix (chain 2), approximately parallel to the lipid bilayer (~5° from the membrane plane) and the short helix (chain 1) forming a ~24° angle with respect to the bilayer plane. Since the peptide does not disrupt the macroscopic alignment of charged or zwitterionic lipid bilayers at lipid-to-protein molar ratio of 50:1, it is possible that higher peptide concentrations might be needed for pore formation, or alternatively, distinctin elicits its cell disruption action by another mechanism.
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