ArticleEuropean biophysics journal : EBJ2017
Oligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy.
Article in European biophysics journal : EBJ, 2017. 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.
- β-Hairpin Antimicrobial Peptides: Class Diversity and Sequence Analysis.ACS infectious diseases · 2026Review
- Antimicrobial Peptides in Focus: Functional Potential and Translational Evidence from Swine Systems.ACS omega · 2025Review
- SAAP-148 Oligomerizes into a Hexamer Forming a Hydrophobic Inner Core.Chembiochem : a European journal of chemical biology · 2025Article
- HSQC-NMR spectroscopy and exploratory data analysis of crude oil residue in relation to the time of spill.RSC advances · 2025Article
- Antimicrobial Peptides: Mechanisms, Applications, and Therapeutic Potential.Infection and drug resistance · 2025Review
- Antimicrobial peptide-based strategies to overcome antimicrobial resistance.Archives of microbiology · 2024Review
- Design of Protegrin-1 Analogs with Improved Antibacterial Selectivity.Pharmaceutics · 2023Article
- Unraveling the Mechanism of Platelet Aggregation Suppression by Monoterpenoids.Bioengineering (Basel, Switzerland) · 2022Article
- Experimental and Computational Characterization of Oxidized and Reduced Protegrin Pores in Lipid Bilayers.The Journal of membrane biology · 2020Article
- Revealing the Mechanisms of Synergistic Action of Two Magainin Antimicrobial Peptides.Frontiers in medical technology · 2020Review
- Article
- Biophysical Investigations Elucidating the Mechanisms of Action of Antimicrobial Peptides and Their Synergism.Biomolecules · 2018Review
- Transmembrane Pore Structures of β-Hairpin Antimicrobial Peptides by All-Atom Simulations.The journal of physical chemistry. B · 2017Article
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Authors and funding
6 authors.
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Abstract
Protegrin pore formation is believed to occur in a stepwise fashion that begins with a nonspecific peptide interaction with the negatively charged bacterial cell walls via hydrophobic and positively charged amphipathic surfaces. There are five known nature protegrins (PG1-PG5), and early studies of PG-1 (PDB ID:1PG1) shown that it could form antiparallel dimer in membrane mimicking environment which could be a first step for further oligomeric membrane pore formation. Later, we solved PG-2 (PDB ID:2MUH) and PG-3 (PDB ID:2MZ6) structures in the same environment and for PG-3 observed a strong d
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