ArticleBiophysical journal2009
Structure and membrane interactions of the antibiotic peptide dermadistinctin K by multidimensional solution and 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 16 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
16 citing papers in PubMed, 46 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
- Programmable Helicity and Macrocycle Symmetry in β-Peptides via Site-Selective Thioamide Substitution.Journal of the American Chemical Society · 2025Article
- Article
- Lipid-Mediated Interactions between the Antimicrobial Peptides Magainin 2 and PGLa in Bilayers.Biophysical journal · 2018Article
- LyeTxI-b, a Synthetic Peptide Derived FromFrontiers in microbiology · 2018Article
- Structural Characterization of the Amyloid Precursor Protein Transmembrane Domain and Its γ-Cleavage Site.ACS omega · 2017Article
- Structure and membrane interactions of the homodimeric antibiotic peptide homotarsinin.Scientific reports · 2017Article
- Ocellatin peptides from the skin secretion of the South American frogThe journal of venomous animals and toxins including tropical diseases · 2017Article
- 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
- Membrane interactions of phylloseptin-1, -2, and -3 peptides by oriented solid-state NMR spectroscopy.Biophysical journal · 2014Article
- (31)P solid-state NMR based monitoring of permeation of cell penetrating peptides into skin.European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V · 2014Article
- Structure and topology of the huntingtin 1-17 membrane anchor by a combined solution and solid-state NMR approach.Biophysical journal · 2013Article
- Elastin, a novel extracellular matrix protein adhering to mycobacterial antigen 85 complex.The Journal of biological chemistry · 2013Article
- Activity determinants of helical antimicrobial peptides: a large-scale computational study.PloS one · 2013Article
- NMR structures of the histidine-rich peptide LAH4 in micellar environments: membrane insertion, pH-dependent mode of antimicrobial action, and DNA transfection.Biophysical journal · 2010Article
- Membrane structure and conformational changes of the antibiotic heterodimeric peptide distinctin by solid-state NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DD K, a peptide first isolated from the skin secretion of the Phyllomedusa distincta frog, has been prepared by solid-phase chemical peptide synthesis and its conformation was studied in trifluoroethanol/water as well as in the presence of sodium dodecyl sulfate and dodecylphosphocholine micelles or small unilamellar vesicles. Multidimensional solution NMR spectroscopy indicates an alpha-helical conformation in membrane environments starting at residue 7 and extending to the C-terminal carboxyamide. Furthermore, DD K has been labeled with (15)N at a single alanine position that is located within the helical core region of the sequence. When reconstituted into oriented phosphatidylcholine membranes the resulting (15)N solid-state NMR spectrum shows a well-defined helix alignment parallel to the membrane surface in excellent agreement with the amphipathic character of DD K. Proton-decoupled (31)P solid-state NMR spectroscopy indicates that the peptide creates a high level of disorder at the level of the phospholipid headgroup suggesting that DD K partitions into the bilayer where it severely disrupts membrane packing.
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Registered trials
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.