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Clustering of Spin-Labeled Molecules in Membranes: What Information Can Be Obtained From Electron-Electron Double Resonance.

Λεπτομέρειες βιβλιογραφικής εγγραφής
Τίτλος: Clustering of Spin-Labeled Molecules in Membranes: What Information Can Be Obtained From Electron-Electron Double Resonance.
Συγγραφείς: Dzuba SA; Institute of Chemical Kinetics and Combustion, Russian Academy of Sciences, Novosibirsk, Russia.
Πηγή: Journal of peptide science : an official publication of the European Peptide Society [J Pept Sci] 2026 Jun; Vol. 32 (6), pp. e70103.
Τύπος έκδοσης: Journal Article; Review
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: John Wiley & Sons Country of Publication: England NLM ID: 9506309 Publication Model: Print Cited Medium: Internet ISSN: 1099-1387 (Electronic) Linking ISSN: 10752617 NLM ISO Abbreviation: J Pept Sci Subsets: MEDLINE
Imprint Name(s): Original Publication: Chichester, West Sussex, UK : John Wiley & Sons, c1995-
Ιατρικοί όροι (MeSH): Cell Membrane*/chemistry , Antimicrobial Peptides*/chemistry , Spin Labels*, Electron Spin Resonance Spectroscopy/methods
Περίληψη: Clustering of antimicrobial peptides (AMPs) in bacterial membranes is a key step in the formation of nanoscale pores within them, which may underlie their bactericidal action. Double electron-electron resonance (DEER, also known as PELDOR) is a pulsed electron paramagnetic resonance (EPR) technique that has a unique ability to study distances between spin labels in the nanometer range. DEER has been successfully applied to the study of the conformations of doubly spin-labeled biomolecules; however, when applied to clusters with a number of spin labels N > 2, DEER encounters certain difficulties both in the proper implementation of measurements and in the interpretation of the data. This paper analyzes these emerging issues and provides recommendations on the proper use of the DEER method and the interpretation of its data when studying clusters of spin-labeled molecules. It demonstrates how the results of studies of AMP clusters in model membranes can be reinterpreted.
(© 2026 European Peptide Society and John Wiley & Sons Ltd.)
References: M. E. Büyükkiraz and Z. Kesmen, “Antimicrobial Peptides (AMPs): A Promising Class of Antimicrobial Compounds,” Journal of Applied Microbiology 132 (2022): 1573–1596.
R. Seyfi, F. A. Kahaki, T. Ebrahimi, et al., “Antimicrobial Peptides (AMPs): Roles, Functions and Mechanism of Action,” International Journal of Peptide Research and Therapeutics 26 (2020): 1451–1463.
H. K. Kang, C. Kim, C. H. Seo, and Y. Park, “The Therapeutic Applications of Antimicrobial Peptides (AMPs): A Patent Review,” Journal of Microbiology 55 (2017): 1–12.
G. S. Dijksteel, M. M. Ulrich, E. Middelkoop, and B. K. Boekema, “Lessons Learned From Clinical Trials Using Antimicrobial Peptides (AMPs),” Frontiers in Microbiology 12 (2021): 616979.
K. A. Brogden, “Antimicrobial Peptides: Pore Formers or Metabolic Inhibitors in Bacteria?,” Nature Reviews Microbiology 3 (2005): 238–250.
L. Thøgersen, B. Schiøtt, T. Vosegaard, N. C. Nielsen, and E. Tajkhorshid, “Peptide Aggregation and Pore Formation in a Lipid Bilayer: A Combined Coarse‐Grained and All Atom Molecular Dynamics Study,” Biophysical Journal 95 (2008): 4337–4347.
C. Wei and A. Pohorille, “Multi‐Oligomeric States of Alamethicin Ion Channel: Assemblies and Conductance,” Biophysical Journal 122 (2023): 2531–2543.
J. D. Richardson and R. C. Van Lehn, “Free Energy Analysis of Peptide‐Induced Pore Formation in Lipid Membranes by Bridging Atomistic and Coarse‐Grained Simulations,” Journal of Physical Chemistry B 128 (2024): 8737–8752.
J. D. Hale and R. E. Hancock, “Alternative Mechanisms of Action of Cationic Antimicrobial Peptides on Bacteria,” Expert Review of Anti‐Infective Therapy 5 (2007): 951–959.
C. Peggion, F. Formaggio, M. Crisma, R. F. Epand, R. M. Epand, and C. Toniolo, “Trichogin: A Paradigm for Lipopeptaibols,” Journal of Peptide Science 9 (2003): 679–689.
A. D. Milov, Y. D. Tsvetkov, J. Raap, M. De Zotti, F. Formaggio, and C. Toniolo, “Conformation, Self‐Aggregation, and Membrane Interaction of Peptaibols as Studied by Pulsed Electron Double Resonance (PELDOR) Spectroscopy,” Biopolymers (Peptide Science) 106 (2016): 6–24.
L. Morbiato, D. S. Haneen, F. Formaggio, and M. De Zotti, “Total Synthesis of the Natural, Medium‐Length, Peptaibol Pentadecaibin and Study of the Chemical Features Responsible for Its Membrane Activity,” Journal of Peptide Science 29 (2023): e3479.
M. Crisma, V. Monaco, F. Formaggio, C. Toniolo, C. George, and J. L. Flippen‐Anderson, “Crystallographic Structure of a Helical Lipopeptaibol Antibiotic Analogue,” Letters in Peptide Science 4 (1997): 213–218.
V. Monaco, F. Formaggio, M. Crisma, C. Toniolo, P. Hanson, and G. L. Millhauser, “Orientation and Immersion Depth of a Helical Lipopeptaibol in Membranes Using TOAC as an ESR Probe,” Biopolymers 50 (1999): 239–253.
A. D. Milov, A. G. Maryasov, and Y. D. Tsvetkov, “Pulsed Electron Double Resonance (PELDOR) and Its Applications in Free‐Radicals Research,” Applied Magnetic Resonance 15 (1998): 107–143.
O. Schiemann and T. F. Prisner, “Long‐Range Distance Determinations in Biomacromolecules by EPR Spectroscopy,” Quarterly Reviews of Biophysics 40 (2007): 1–53.
G. Jeschke, “DEER Distance Measurements on Proteins,” Annual Review of Physical Chemistry 63 (2012): 419–446.
Y. D. Tsvetkov, M. K. Bowman, and Y. A. Grishin, Pulsed electron–electron double resonance (Springer, 2019).
O. Schiemann, C. A. Heubach, D. Abdullin, et al., “Benchmark Test and Guidelines for DEER/PELDOR Experiments on Nitroxide‐Labeled Biomolecules,” Journal of the American Chemical Society 143 (2021): 17875–17890.
B. Joseph, E. A. Jaumann, A. Sikora, K. Barth, T. F. Prisner, and D. S. Cafiso, “In Situ Observation of Conformational Dynamics and Protein Ligand–Substrate Interactions in Outer‐Membrane Proteins With DEER/PELDOR Spectroscopy,” Nature Protocols 14 (2019): 2344–2369.
I. D. Sahu and G. A. Lorigan, “Electron Paramagnetic Resonance as a Tool for Studying Membrane Proteins,” Biomolecules (Basel) 10 (2020): 763.
M. H. Tessmer and S. Stoll, “Protein Modeling With DEER Spectroscopy,” Annual Review of Biophysics 54 (2025): 35–57.
T. А. Von Hagens, Y. Polyhach, M. Sajid, A. Godt, and G. Jeschke, “Suppression of Ghost Distances in Multiple‐Spin Double Electron–Electron Resonance,” Physical Chemistry Chemical Physics 15 (2013): 5854–5866.
В. Giannoulis, R. Ward, E. Branigan, J. H. Naismith, and B. E. Bode, “PELDOR in Rotationally Symmetric Homo‐Oligomers,” Molecular Physics 111 (2013): 2845–2854.
G. Jeschke, M. Sajid, M. Schulte, and A. Godt, “Three‐Spin Correlations in Double Electron–Electron Resonance,” Physical Chemistry Chemical Physics 11 (2009): 6580–6591.
A. S. Kashnik, D. S. Baranov, and S. A. Dzuba, “Spatial Arrangement of the Drug Ibuprofen in a Model Membrane in the Presence of Lipid Rafts,” Journal of Physical Chemistry B 128 (2024): 3652–3661.
A. S. Kashnik, A. N. Atnyukova, D. S. Baranov, and S. A. Dzuba, “DEER Study of Spatial Arrangement of Spin‐Labeled Diclofenac in Lipid Bilayers of Different Composition,” Applied Magnetic Resonance 55 (2024): 1145–1157.
E. A. Golysheva, A. S. Kashnik, D. S. Baranov, and S. A. Dzuba, “Nanoclusters of Guest Molecules in Lipid Rafts of a Model Membrane Revealed by Pulsed Dipolar EPR Spectroscopy,” Journal of Physical Chemistry B 129 (2025): 650–658.
S. A. Dzuba, “Pulsed Dipolar EPR Spectroscopy of Nanometer‐Sized Oligomers and Clusters of Molecules,” Russian Chemical Reviews 94 (2025): RCR5198.
A. D. Milov, Y. A. Grishin, S. A. Dzuba, and Y. D. Tsvetkov, “Effect of Pumping Pulse Duration on Echo Signal Amplitude in Four‐Pulse PELDOR,” Applied Magnetic Resonance 41 (2011): 59–67.
S. A. Dzuba, “Conducting a Three‐Pulse DEER Experiment Without Dead Time: A Review,” Journal of Magnetic Resonance Open 14–15 (2023): 100100.
K. M. Salikhov, S. A. Dzuba, and A. M. Raitsimring, “The Theory of Electron Spin Echo Signal Decay Resulting From Dipole‐Dipole Interactions Between Paramagnetic Centers in Solids,” Journal of Magnetic Resonance (1969) 42 (1981): 255–276.
K. M. Salikhov, I. T. Khairuzhdinov, and R. B. Zaripov, “Three‐Pulse ELDOR Theory Revisited,” Applied Magnetic Resonance 45 (2014): 573–619.
K. M. Salikhov and I. T. Khairuzhdinov, “Four‐Pulse ELDOR Theory of the Spin ½ Label Pairs Extended to Overlapping EPR Spectra and to Overlapping Pump and Observer Excitation Bands,” Applied Magnetic Resonance 46 (2015): 67–83.
E. A. Golysheva, A. S. Smorygina, and S. A. Dzuba, “Double Electron–Electron Resonance vs. Instantaneous Diffusion Effect on Spin‐Echo for Nitroxide Spins Labels,” Applied Magnetic Resonance 53 (2022): 685–698.
M. Bretschneider, B. Endeward, J. Plackmeyer, and T. F. Prisner, “Using PELDOR to Count Spins on Multi‐Nitroxides,” Journal of Magnetic Resonance 375 (2025): 107886.
V. N. Syryamina, N. E. Sannikova, M. De Zotti, M. Gobbo, F. Formaggio, and S. A. Dzuba, “Tylopeptin B Peptide Antibiotic in Lipid Membranes at Low Concentrations: Self‐Assembling, Mutual Repulsion and Localization,” Biochimica et Biophysica Acta (BBA) ‐ Biomembranes 1863 (2021): 183585.
G. Jeschke, V. Chechik, P. Ionita, et al., “DeerAnalysis2006—A Comprehensive Software Package for Analyzing Pulsed ELDOR Data,” Applied Magnetic Resonance 30 (2006): 473–498.
Grant Information: 25-23-00061 Russian Science Foundation
Substance Nomenclature: 0 (Spin Labels)
0 (Antimicrobial Peptides)
Entry Date(s): Date Created: 20260516 Date Completed: 20260716 Latest Revision: 20260811
Update Code: 20260812
DOI: 10.1002/psc.70103
PMID: 42141744
Βάση Δεδομένων: MEDLINE
Περιγραφή
ISSN:1099-1387
DOI:10.1002/psc.70103