ArticleJournal of biomolecular NMR2015
High-resolution NMR structure of the antimicrobial peptide protegrin-2 in the presence of DPC micelles.
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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13 citing papers in PubMed, 26 citations in OpenAlex.
- Dimerization of the β-Hairpin Membrane-Active Cationic Antimicrobial Peptide Capitellacin from Marine Polychaeta: An NMR Structural and Thermodynamic Study.Biomolecules · 2024Article
- Binding of Different Cyclosporin Variants to Micelles Evidenced by NMR and MD Simulations.Membranes · 2023Article
- Protegrin-2, a potential inhibitor for targeting SARS-CoV-2 main protease MComputational and structural biotechnology journal · 2023Article
- Molecular Recognition of Imidazole Derivatives by Co(III)-Porphyrinsin Phosphate Buffer (pH = 7.4) and Cetylpyridinium Chloride Containing Solutions.Molecules (Basel, Switzerland) · 2021Article
- Antimicrobial Peptides in Farm Animals: An Updated Review on Its Diversity, Function, Modes of Action and Therapeutic Prospects.Veterinary sciences · 2020Review
- Membrane Active Peptides and Their Biophysical Characterization.Biomolecules · 2018Review
- Article
- In silico optimization of a guava antimicrobial peptide enables combinatorial exploration for peptide design.Nature communications · 2018Article
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- Oligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy.European biophysics journal : EBJ · 2017Article
- Micelle-Triggered β-Hairpin to α-Helix Transition in a 14-Residue Peptide from a Choline-Binding Repeat of the Pneumococcal Autolysin LytA.Chemistry (Weinheim an der Bergstrasse, Germany) · 2015Article
- Antimicrobial peptide protegrin-3 adopt an antiparallel dimer in the presence of DPC micelles: a high-resolution NMR study.Journal of biomolecular NMR · 2015Article
- NMR studies of membrane proteins.Journal of biomolecular NMR · 2015Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PG-1 adopts a dimeric structure in dodecylphosphocholine (DPC) micelles, and a channel is formed by the association of several dimers but the molecular mechanisms of the membrane damage by non-α-helical peptides are still unknown. The formation of the PG-1 dimer is important for pore formation in the lipid bilayer, since the dimer can be regarded as the primary unit for assembly into the ordered aggregates. It was supposed that only 12 residues (RGGRL-CYCRR-RFCVC-V) are needed to endow protegrin molecules with strong antibacterial activity and that at least four additional residues are needed to add potent antifungal properties. Thus, the 16-residue protegrin (PG-2) represents the minimal structure needed for broad-spectrum antimicrobial activity encompassing bacteria and fungi. As the peptide conformation and peptide-to-membrane binding properties are very sensitive to single amino acid substitutions, the solution structure of PG-2 in solution and in a membrane mimicking environment are crucial. In order to find evidence if the oligomerization state of PG-1 in a lipid environment will be the same or not for another protegrins, we investigate in the present work the PG-2 NMR solution structure in the presence of perdeuterated DPC micelles. The NMR study reported in the present work indicates that PG-2 form a well-defined structure (PDB: 2MUH) composed of a two-stranded antiparallel β-sheet when it binds to DPC micelles.
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