ArticleBiophysical journal2004
Structure of (KIAGKIA)3 aggregates in phospholipid bilayers by solid-state NMR.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Three Decades of REDOR in Protein Science: A Solid-State NMR Technique for Distance Measurement and Spectral Editing.International journal of molecular sciences · 2023Review
- From Angstroms to Nanometers: Measuring Interatomic Distances by Solid-State NMR.Chemical reviews · 2022Review
- Localization Preference of Antimicrobial Peptides on Liquid-Disordered Membrane Domains.Frontiers in cell and developmental biology · 2020Article
- Coarse-grained simulations of hemolytic peptide δ-lysin interacting with a POPC bilayer.Biochimica et biophysica acta · 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
- Hydrophobic mismatch demonstrated for membranolytic peptides, and their use as molecular rulers to measure bilayer thickness in native cells.Scientific reports · 2015Article
- REDOR NMR for drug discovery.Bioorganic & medicinal chemistry letters · 2013Article
- Reorientation and dimerization of the membrane-bound antimicrobial peptide PGLa from microsecond all-atom MD simulations.Biophysical journal · 2012Article
- Antimicrobial and cell-penetrating peptides induce lipid vesicle fusion by folding and aggregation.European biophysics journal : EBJ · 2012Article
- Does cholesterol play a role in the bacterial selectivity of antimicrobial peptides?Frontiers in immunology · 2012Article
- A kinked antimicrobial peptide from Bombina maxima. II. Behavior in phospholipid bilayers.European biophysics journal : EBJ · 2011Article
- Lipid-protein correlations in nanoscale phospholipid bilayers determined by solid-state nuclear magnetic resonance.Biochemistry · 2010Article
- Probing the "charge cluster mechanism" in amphipathic helical cationic antimicrobial peptides.Biochemistry · 2010Article
- A refinement protocol to determine structure, topology, and depth of insertion of membrane proteins using hybrid solution and solid-state NMR restraints.Journal of biomolecular NMR · 2009Article
- Article
- Molecular dynamics simulations of model trans-membrane peptides in lipid bilayers: a systematic investigation of hydrophobic mismatch.Biophysical journal · 2006Article
- Solid-state NMR analysis of the PGLa peptide orientation in DMPC bilayers: structural fidelity of 2H-labels versus high sensitivity of 19F-NMR.Biophysical journal · 2006Article
- Concentration-dependent realignment of the antimicrobial peptide PGLa in lipid membranes observed by solid-state 19F-NMR.Biophysical journal · 2005Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors.
Funding
Abstract
The interchain (13)C-(19)F dipolar coupling measured in a rotational-echo double-resonance (REDOR) experiment performed on mixtures of differently labeled KIAGKIA-KIAGKIA-KIAGKIA (K3) peptides (one specifically (13)C labeled, and the other specifically (19)F labeled) in multilamellar vesicles of dipalmitoylphosphatidylcholine and dipalmitoylphosphatidylglycerol (1:1) shows that K3 forms close-packed clusters, primarily dimers, in bilayers at a lipid/peptide molar ratio (L/P) of 20. Dipolar coupling to additional peptides is weaker than that within the dimers, consistent with aggregates of monomers and dimers. Analysis of the sideband dephasing rates indicates a preferred orientation between the peptide chains of the dimers. The combination of the distance and orientation information from REDOR is consistent with a parallel (N-N) dimer structure in which two K3 helices intersect at a cross-angle of approximately 20 degrees. Static (19)F NMR experiments performed on K3 in oriented lipid bilayers show that between L/P = 200 and L/P = 20, K3 chains change their absolute orientation with respect to the membrane normal. This result suggests that the K3 dimers detected by REDOR at L/P = 20 are not on the surface of the bilayer but are in a membrane pore.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.