ArticleBiophysical journal2006
Utilizing ESEEM spectroscopy to locate the position of specific regions of membrane-active peptides within model membranes.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 61 citations in OpenAlex.
- EPR spectroscopy reveals glycerol-dependent activation of cysteamine dioxygenase (ADO) enables bidentate substrate coordination.The Journal of biological chemistry · 2026Article
- Advances in EPR Approaches for Studying Structural Properties of Membrane Proteins.Magnetic resonance in chemistry : MRC · 2026Review
- Membrane Depth Measurements of E Protein byBiophysica · 2025Article
- Metal Ion Dynamic Nuclear Polarization in Mn(II)-Doped CdS Nanocrystals: Atomic-Scale Investigation of the Dopant and Its Host.ACS nano · 2025Article
- Comparison of lipid dynamics and permeability in styrene-maleic acid and diisobutylene-maleic acid copolymer lipid nanodiscs by electron paramagnetic resonance spectroscopy.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Article
- Application of DNP-enhanced solid-state NMR to studies of amyloid-β peptide interaction with lipid membranes.Chemistry and physics of lipids · 2021Article
- Electron Spin Relaxation of Photoexcited Porphyrin in Water-Glycerol Glass.Molecules (Basel, Switzerland) · 2020Article
- Topology of active, membrane-embedded Bax in the context of a toroidal pore.Cell death and differentiation · 2018Article
- Site-Directed Spin Labeling EPR for Studying Membrane Proteins.BioMed research international · 2018Review
- Conformational Changes Underlying Desensitization of the Pentameric Ligand-Gated Ion Channel ELIC.Structure (London, England : 1993) · 2015Article
- Determining the Secondary Structure of Membrane Proteins and Peptides Via Electron Spin Echo Envelope Modulation (ESEEM) Spectroscopy.Methods in enzymology · 2015Article
- Probing water density and dynamics in the chaperonin GroEL cavity.Journal of the American Chemical Society · 2014Article
- Solid-state NMR (31)P paramagnetic relaxation enhancement membrane protein immersion depth measurements.The journal of physical chemistry. B · 2014Article
- Electron Paramagnetic Resonance and Electron Spin Echo Studies of CoApplied magnetic resonance · 2013Article
- Molecular dynamics simulations of depth distribution of spin-labeled phospholipids within lipid bilayer.The journal of physical chemistry. B · 2013Article
- ESR study of interfacial hydration layers of polypeptides in water-filled nanochannels and in vitrified bulk solvents.PloS one · 2013Article
- Probing the structure of membrane proteins with electron spin echo envelope modulation spectroscopy.Protein science : a publication of the Protein Society · 2011Article
- Solid-state NMR paramagnetic relaxation enhancement immersion depth studies in phospholipid bilayers.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2010Article
- Electron spin-echo envelope modulation (ESEEM) reveals water and phosphate interactions with the KcsA potassium channel.Biochemistry · 2010Article
- Pulsed EPR determination of water accessibility to spin-labeled amino acid residues in LHCIIb.Biophysical journal · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane-active peptides participate in many cellular processes, and therefore knowledge of their mode of interaction with phospholipids is essential for understanding their biological function. Here we present a new methodology based on electron spin-echo envelope modulation to probe, at a relatively high resolution, the location of membrane-bound lytic peptides and to study their effect on the water concentration profile of the membrane. As a first example, we determined the location of the N-terminus of two membrane-active amphipathic peptides, the 26-mer bee venom melittin and a de novo designed 15-mer D,L-amino acid amphipathic peptide (5D-L9K6C), both of which are antimicrobial and bind and act similarly on negatively charged membranes. A nitroxide spin label was introduced to the N-terminus of the peptides and measurements were performed either in H2O solutions with deuterated model membranes or in D2O solutions with nondeuterated model membranes. The lipids used were dipalmitoyl phosphatidylcholine (DPPC) and phosphatidylglycerol (PG), (DPPC/PG (7:3 w/w)), egg phosphatidylcholine (PC) and PG (PC/PG (7:3 w/w)), and phosphatidylethanolamine (PE) and PG (PE/PG, 7:3w/w). The modulation induced by the 2H nuclei was determined and compared with a series of controls that produced a reference "ruler". Actual estimated distances were obtained from a quantitative analysis of the modulation depth based on a simple model of an electron spin situated at a certain distance from the bottom of a layer with homogeneously distributed deuterium nuclei. The N-terminus of both peptides was found to be in the solvent layer in both the DPPC/PG and PC/PG membranes. For PE/PG, a further displacement into the solvent was observed. The addition of the peptides was found to change the water distribution in the membrane, making it "flatter" and increasing the penetration depth into the hydrophobic region.
Indexed as
Identifiers
What OpenQuestion holds
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.