ArticleBiophysical journal2006
Interaction of protegrin-1 with lipid bilayers: membrane thinning effect.
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 32 papers.
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Who cites it
32 citing papers in PubMed, 70 citations in OpenAlex.
- Flowering Poration-A Synergistic Multi-Mode Antibacterial Mechanism by a Bacteriocin Fold.iScience · 2020Article
- Experimental and Computational Characterization of Oxidized and Reduced Protegrin Pores in Lipid Bilayers.The Journal of membrane biology · 2020Article
- Antimicrobial peptide ROAD-1 triggers phase change in local membrane environment to execute its activity.Journal of molecular modeling · 2019Article
- Transmembrane Pore Structures of β-Hairpin Antimicrobial Peptides by All-Atom Simulations.The journal of physical chemistry. B · 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
- Computational Methods for Structural and Functional Studies of Alzheimer's Amyloid Ion Channels.Methods in molecular biology (Clifton, N.J.) · 2016Article
- Membrane Thinning and Thickening Induced by Membrane-Active Amphipathic Peptides.Frontiers in cell and developmental biology · 2016Article
- Implicit Membrane Investigation of the Stability of Antimicrobial Peptide β-Barrels and Arcs.The Journal of membrane biology · 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
- High-resolution NMR structure of the antimicrobial peptide protegrin-2 in the presence of DPC micelles.Journal of biomolecular NMR · 2015Article
- Article
- Multiscale Models of Antibiotic Probiotics.Current opinion in chemical engineering · 2014Article
- Substrate-bound outward-open state of the betaine transporter BetP provides insights into Na+ coupling.Nature communications · 2014Article
- Mechanism of membrane permeation induced by synthetic β-hairpin peptides.Biophysical journal · 2013Article
- Membrane binding and insertion of a pHLIP peptide studied by all-atom molecular dynamics simulations.International journal of molecular sciences · 2013Article
- Membrane interactions and pore formation by the antimicrobial peptide protegrin.Biophysical journal · 2013Article
- Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.Journal of chemical theory and computation · 2013Article
- Antimicrobial protegrin-1 forms amyloid-like fibrils with rapid kinetics suggesting a functional link.Biophysical journal · 2011Article
- Knowledge-based computational methods for identifying or designing novel, non-homologous antimicrobial peptides.European biophysics journal : EBJ · 2011Article
- Review
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Protegrins (PG) are important in defending host tissues, preventing infection via an attack on the membrane surface of invading microorganisms. Protegrins have powerful antibiotic abilities, but the molecular-level mechanisms underlying the interactions of their beta-sheet motifs with the membrane are not known. Protegrin-1 (PG-1) is composed of 18 amino acids with a high content of basic residues and two disulfide bonds. Here we focused on the stability of PG-1 at the amphipathic interface in lipid bilayers and on the details of the peptide-membrane interactions. We simulated all-atom models of the PG-1 monomer with explicit water and lipid bilayers composed of both homogeneous POPC (palmitoyl-oleyl-phosphatidylcholine) lipids and a mixture of POPC/POPG (palmitoyl-oleyl-phosphatidylglycerol) (4:1) lipids. We observed that local thinning of the lipid bilayers mediated by the peptide is enhanced in the lipid bilayer containing POPG, consistent with experimental results of selective membrane targeting. The beta-hairpin motif of PG-1 is conserved in both lipid settings, whereas it is highly bent in aqueous solution. The conformational dynamics of PG-1, especially the highly charged beta-hairpin turn region, are found to be mostly responsible for disturbing the membrane. Even though the eventual membrane disruption requires PG-1 oligomers, our simulations clearly show the first step of the monomeric effects. The thinning effects in the bilayer should relate to pore/channel formation in the lipid bilayer and thus be responsible for further defects in the membrane caused by oligomer.
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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.