ArticleBiophysical journal2005
Concentration-dependent realignment of the antimicrobial peptide PGLa in lipid membranes observed by solid-state 19F-NMR.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 151 citations in OpenAlex.
- Replica Exchange Molecular Dynamics with Hydrogen Mass Repartitioning Improves Sampling of Peptide Binding to a Lipid Bilayer.Journal of chemical theory and computation · 2026Article
- DOPC Liposomal Formulation of Antimicrobial Peptide LL17-32 with Reduced Cytotoxicity: A Promising Carrier AgainstPharmaceutics · 2025Article
- Article
- Binding and dimerization of PGLa peptides in anionic lipid bilayer studied by replica exchange molecular dynamics.Scientific reports · 2024Article
- The Functionality of Membrane-Inserting Proteins and Peptides: Curvature Sensing, Generation, and Pore Formation.The Journal of membrane biology · 2023Review
- Recent Progress in the Discovery and Design of Antimicrobial Peptides Using Traditional Machine Learning and Deep Learning.Antibiotics (Basel, Switzerland) · 2022Review
- Membranolytic Mechanism of Amphiphilic Antimicrobial β-Stranded [KL]Biomedicines · 2022Article
- Concerted Rolling and Penetration of Peptides during Membrane Binding.Journal of chemical theory and computation · 2022Article
- Probing and Manipulating the Lateral Pressure Profile in Lipid Bilayers Using Membrane-Active Peptides-A Solid-StateInternational journal of molecular sciences · 2022Article
- Membrane Interactions of Latarcins: Antimicrobial Peptides from Spider Venom.International journal of molecular sciences · 2021Article
- Overlapping Properties of the Short Membrane-Active Peptide BP100 With (i) Polycationic TAT and (ii) α-helical Magainin Family Peptides.Frontiers in cellular and infection microbiology · 2021Article
- Cholesterol Alters the Orientation and Activity of the Influenza Virus M2 Amphipathic Helix in the Membrane.The journal of physical chemistry. B · 2020Article
- Chiral supramolecular architecture of stable transmembrane pores formed by an α-helical antibiotic peptide in the presence of lyso-lipids.Scientific reports · 2020Article
- Review
- Binding and Flip as Initial Steps for BP-100 Antimicrobial Actions.Scientific reports · 2019Article
- Molecular mechanism of synergy between the antimicrobial peptides PGLa and magainin 2.Scientific reports · 2017Article
- Charged Antimicrobial Peptides Can Translocate across Membranes without Forming Channel-like Pores.Biophysical journal · 2017Article
- Orientation and Location of the Cyclotide Kalata B1 in Lipid Bilayers Revealed by Solid-State NMR.Biophysical journal · 2017Article
- Article
- Homo- and heteromeric interaction strengths of the synergistic antimicrobial peptides PGLa and magainin 2 in membranes.European biophysics journal : EBJ · 2016Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The membrane-disruptive antimicrobial peptide PGLa is found to change its orientation in a dimyristoyl-phosphatidylcholine bilayer when its concentration is increased to biologically active levels. The alignment of the alpha-helix was determined by highly sensitive solid-state NMR measurements of (19)F dipolar couplings on CF(3)-labeled side chains, and supported by a nonperturbing (15)N label. At a low peptide/lipid ratio of 1:200 the amphiphilic peptide resides on the membrane surface in the so-called S-state, as expected. However, at high peptide concentration (>/=1:50 molar ratio) the helix axis changes its tilt angle from approximately 90 degrees to approximately 120 degrees , with the C-terminus pointing toward the bilayer interior. This tilted "T-state" represents a novel feature of antimicrobial peptides, which is distinct from a membrane-inserted I-state. At intermediate concentration, PGLa is in exchange between the S- and T-state in the timescale of the NMR experiment. In both states the peptide molecules undergo fast rotation around the membrane normal in liquid crystalline bilayers; hence, large peptide aggregates do not form. Very likely the obliquely tilted T-state represents an antiparallel dimer of PGLa that is formed in the membrane at increasing concentration.
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