ArticleBiophysical journal2006
Solid-state NMR analysis of the PGLa peptide orientation in DMPC bilayers: structural fidelity of 2H-labels versus high sensitivity of 19F-NMR.
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 36 papers.
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Who cites it
36 citing papers in PubMed.
- Predicting peptide orientation in membrane interactions: a review on transmembrane and surface-bound states.European biophysics journal : EBJ · 2026Review
- Chemically diverse antimicrobial peptides induce hyperpolarization of the E. coli membrane.Communications biology · 2024Article
- A Critical Review of Short Antimicrobial Peptides from Scorpion Venoms, Their Physicochemical Attributes, and Potential for the Development of New Drugs.The Journal of membrane biology · 2024Review
- Microbial- and Plant-Derived Bioactive Peptides and Their Applications against Foodborne Pathogens: Current Status and Future Prospects.International journal of microbiology · 2024Review
- Antimicrobial Proteins: Structure, Molecular Action, and Therapeutic Potential.Pharmaceutics · 2022Review
- Tilted State Population of Antimicrobial Peptide PGLa Is Coupled to the Transmembrane Potential.Journal of chemical information and modeling · 2022Article
- Probing and Manipulating the Lateral Pressure Profile in Lipid Bilayers Using Membrane-Active Peptides-A Solid-StateInternational journal of molecular sciences · 2022Article
- Antimicrobial peptides: mechanism of action, activity and clinical potential.Military Medical Research · 2021Review
- 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
- Chiral supramolecular architecture of stable transmembrane pores formed by an α-helical antibiotic peptide in the presence of lyso-lipids.Scientific reports · 2020Article
- 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
- Action of Antimicrobial Peptides on Bacterial and Lipid Membranes: A Direct Comparison.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
- Molecular dynamics simulations on PGLa using NMR orientational constraints.Journal of biomolecular NMR · 2015Article
- 3D hydrophobic moment vectors as a tool to characterize the surface polarity of amphiphilic peptides.Biophysical journal · 2014Article
- Structure analysis and conformational transitions of the cell penetrating peptide transportan 10 in the membrane-bound state.PloS one · 2014Article
- Synergistic insertion of antimicrobial magainin-family peptides in membranes depends on the lipid spontaneous curvature.Biophysical journal · 2013Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The structure and alignment of the amphipathic alpha-helical antimicrobial peptide PGLa in a lipid membrane is determined with high accuracy by solid-state 2H-NMR. Orientational constraints are derived from a series of eight alanine-3,3,3-d3-labeled peptides, in which either a native alanine is nonperturbingly labeled (4x), or a glycine (2x) or isoleucine (2x) is selectively replaced. The concentration dependent realignment of the alpha-helix from the surface-bound "S-state" to a tilted "T-state" by 30 degrees is precisely calculated using the quadrupole splittings of the four nonperturbing labels as constraints. The remaining, potentially perturbing alanine-3,3,3-d3 labels show only minor deviations from the unperturbed peptide structure and help to single out the unique solution. Comparison with previous 19F-NMR constraints from 4-CF3-phenylglycine labels shows that the structure and orientation of the PGLa peptide is not much disturbed even by these bulky nonnatural side chains, which contain CF3 groups that offer a 20-fold better NMR sensitivity than CD3 groups.
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