ArticleJournal of biomolecular NMR2015
Antimicrobial peptide protegrin-3 adopt an antiparallel dimer in the presence of DPC micelles: a high-resolution NMR study.
Article in Journal of biomolecular NMR, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Dimerization of the β-Hairpin Membrane-Active Cationic Antimicrobial Peptide Capitellacin from Marine Polychaeta: An NMR Structural and Thermodynamic Study.Biomolecules · 2024Article
- Unraveling the Mechanism of Platelet Aggregation Suppression by Monoterpenoids.Bioengineering (Basel, Switzerland) · 2022Article
- Molecular Recognition of Imidazole Derivatives by Co(III)-Porphyrinsin Phosphate Buffer (pH = 7.4) and Cetylpyridinium Chloride Containing Solutions.Molecules (Basel, Switzerland) · 2021Article
- Dodecapeptide Cathelicidins of Cetartiodactyla: Structure, Mechanism of Antimicrobial Action, and Synergistic Interaction With Other Cathelicidins.Frontiers in microbiology · 2021Article
- Experimental and Computational Characterization of Oxidized and Reduced Protegrin Pores in Lipid Bilayers.The Journal of membrane biology · 2020Article
- Effect of triphenylphosphonium moiety on spatial structure and biointeractions of stereochemical variants of YRFK motif.European biophysics journal : EBJ · 2019Article
- Evidence of oligomerization of bovine insulin in solution given by NMR.European biophysics journal : EBJ · 2018Article
- Article
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- Transmembrane Pore Structures of β-Hairpin Antimicrobial Peptides by All-Atom Simulations.The journal of physical chemistry. B · 2017Article
- Computational studies of peptide-induced membrane pore formation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Oligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy.European biophysics journal : EBJ · 2017Article
- Computational prediction of the optimal oligomeric state for membrane-inserted β-barrels of protegrin-1 and related mutants.Journal of peptide science : an official publication of the European Peptide Society · 2017Article
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6 authors.
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Abstract
A tendency to dimerize in the presence of lipids was found for the protegrin. The dimer formation by the protegrin-1 (PG-1) is the first step for further oligomeric membrane pore formation. Generally there are two distinct model of PG-1 dimerization in either a parallel or antiparallel β-sheet. But despite the wealth of data available today, protegrin dimer structure and pore formation is still not completely understood. In order to investigate a more detailed dimerization process of PG-1 and if it will be the same for another type of protegrins, in this work we used a high-resolution NMR spectroscopy for structure determination of protegrin-3 (RGGGL-CYCRR-RFCVC-VGR) in the presence of perdeuterated DPC micelles and demonstrate that PG-3 forms an antiparallel NCCN dimer with a possible association of these dimers. This structural study complements previously published solution, solid state and computational studies of PG-1 in various environments and validate the potential of mean force simulations of PG-1 dimers and association of dimers to form octameric or decameric β-barrels.
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