ArticleBiophysical journal2009
Structure and alignment of the membrane-associated peptaibols ampullosporin A and alamethicin by oriented 15N and 31P solid-state NMR spectroscopy.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 94 citations in OpenAlex.
- Membrane Topology and Oligomerization of Peptaibols by Solid-State NMR Spectroscopy.Journal of peptide science : an official publication of the European Peptide Society · 2026Review
- Solid-State NMR Approaches to Study Protein Structure and Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Charge, Hydrophobicity, and Lipid Type Drive Antimicrobial Peptides' Unique Perturbation Ensembles.Biochemistry · 2025Article
- Melittin can permeabilize membranes via large transient pores.Nature communications · 2024Article
- Synthesis, Conformational Analysis and Antitumor Activity of the Naturally Occurring Antimicrobial Medium-Length Peptaibol Pentadecaibin and Spin-Labeled Analogs Thereof.International journal of molecular sciences · 2023Article
- Modeling the Structure of Crystalline Alamethicin and Its NMR Chemical Shift Tensors.Antibiotics (Basel, Switzerland) · 2021Article
- Contributions and Limitations of Biophysical Approaches to Study of the Interactions between Amphiphilic Molecules and the Plant Plasma Membrane.Plants (Basel, Switzerland) · 2020Review
- Monitoring the Site-Specific Solid-State NMR Data in Oligopeptides.International journal of molecular sciences · 2020Article
- Review
- Synergistic combination of alkylphosphocholines with peptaibols in targeting Leishmania infantum in vitro.International journal for parasitology. Drugs and drug resistance · 2018Article
- Biophysical Investigations Elucidating the Mechanisms of Action of Antimicrobial Peptides and Their Synergism.Biomolecules · 2018Review
- Dynamic membrane interactions of antibacterial and antifungal biomolecules, and amyloid peptides, revealed by solid-state NMR spectroscopy.Biochimica et biophysica acta. General subjects · 2018Review
- Alamethicin Supramolecular Organization in Lipid Membranes fromBiophysical journal · 2016Article
- Insertion into lipid bilayer of truncated pHLIPBiochemistry and biophysics reports · 2016Article
- Simulations of Membrane-Disrupting Peptides I: Alamethicin Pore Stability and Spontaneous Insertion.Biophysical journal · 2016Article
- Oriented samples: a tool for determining the membrane topology and the mechanism of action of cationic antimicrobial peptides by solid-state NMR.Biophysical reviews · 2015Article
- Dependence of Alamethicin Membrane Orientation on the Solution Concentration.The journal of physical chemistry. C, Nanomaterials and interfaces · 2013Article
- Charge distribution and imperfect amphipathicity affect pore formation by antimicrobial peptides.Biochimica et biophysica acta · 2012Article
- Observing a model ion channel gating action in model cell membranes in real time in situ: membrane potential change induced alamethicin orientation change.Journal of the American Chemical Society · 2012Article
- Mechanisms of peptide-induced pore formation in lipid bilayers investigated by oriented 31P solid-state NMR spectroscopy.PloS one · 2012Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ampullosporin A and alamethicin are two members of the peptaibol family of antimicrobial peptides. These compounds are produced by fungi and are characterized by a high content of hydrophobic amino acids, and in particular the alpha-tetrasubstituted amino acid residue ?-aminoisobutyric acid. Here ampullosporin A and alamethicin were uniformly labeled with (15)N, purified and reconstituted into oriented phophatidylcholine lipid bilayers and investigated by proton-decoupled (15)N and (31)P solid-state NMR spectroscopy. Whereas alamethicin (20 amino acid residues) adopts transmembrane alignments in 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) or 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) membranes the much shorter ampullosporin A (15 residues) exhibits comparable configurations only in thin membranes. In contrast the latter compound is oriented parallel to the membrane surface in 1,2-dimyristoleoyl-sn-glycero-3-phosphocholine and POPC bilayers indicating that hydrophobic mismatch has a decisive effect on the membrane topology of these peptides. Two-dimensional (15)N chemical shift -(1)H-(15)N dipolar coupling solid-state NMR correlation spectroscopy suggests that in their transmembrane configuration both peptides adopt mixed alpha-/3(10)-helical structures which can be explained by the restraints imposed by the membranes and the bulky alpha-aminoisobutyric acid residues. The (15)N solid-state NMR spectra also provide detailed information on the helical tilt angles. The results are discussed with regard to the antimicrobial activities of the peptides.
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