AbstractThe skin secretions of amphibians are a rich source of antimicrobial peptides. The two antimicrobial peptides PGLa and magainin 2, isolated from the African frog Xenopus laevis, have been shown to act synergistically by permeabilizing the membranes of microorganisms. In this report, the literature on PGLa is extensively reviewed, with special focus on its synergistically enhanced activity in the presence of magainin 2. Our recent solid state 2H NMR studies of the orientation of PGLa in lipid membranes alone and in the presence of magainin 2 are described in detail, and some new data from 3,3,3-2H3-L-alanine labeled PGLa are included in the analysis
AbstractPeptidyl-glycine-leucine-carboxyamide (PGLa), isolated from granular skin glands of Xenopus ...
AbstractThe structure and alignment of the amphipathic α-helical antimicrobial peptide PGLa in a lip...
Magainin 2 and PGLa are among the best-studied cationic antimicrobial peptides. They bind preferenti...
AbstractThe skin secretions of amphibians are a rich source of antimicrobial peptides. The two antim...
Magainin and PGLa are 23- and 21-residue peptides isolated from the skin of the African clawed frog ...
Magainin and PGLa are 23- and 21-residue peptides isolated from the skin of the African clawed frog ...
Magainin and PGLa are 23- and 21-residue peptides isolated from the skin of the African clawed frog ...
AbstractThe cationic antimicrobial peptide PGLa is electrostatically attracted to bacterial membrane...
AbstractPGLa and magainin 2 (MAG2) are amphiphilic antimicrobial peptides from frog skin with known ...
AbstractPGLa, a 21-residue member of the magainin family of antibiotic peptides, is shown to be heli...
AbstractUsing two-dimensional NMR spectroscopy, a complete 1H resonance assignment has been obtained...
AbstractThe membrane-active antimicrobial peptide PGLa from Xenopus laevis is known from solid-state...
AbstractTo gain further insight into the antimicrobial activities of cationic linear peptides, we in...
Magainin 2 and PGLa are cationic, amphipathic antimicrobial peptides which when added as equimolar m...
AbstractPGLa and magainin 2 (MAG2) are amphiphilic antimicrobial peptides from frog skin with known ...
AbstractPeptidyl-glycine-leucine-carboxyamide (PGLa), isolated from granular skin glands of Xenopus ...
AbstractThe structure and alignment of the amphipathic α-helical antimicrobial peptide PGLa in a lip...
Magainin 2 and PGLa are among the best-studied cationic antimicrobial peptides. They bind preferenti...
AbstractThe skin secretions of amphibians are a rich source of antimicrobial peptides. The two antim...
Magainin and PGLa are 23- and 21-residue peptides isolated from the skin of the African clawed frog ...
Magainin and PGLa are 23- and 21-residue peptides isolated from the skin of the African clawed frog ...
Magainin and PGLa are 23- and 21-residue peptides isolated from the skin of the African clawed frog ...
AbstractThe cationic antimicrobial peptide PGLa is electrostatically attracted to bacterial membrane...
AbstractPGLa and magainin 2 (MAG2) are amphiphilic antimicrobial peptides from frog skin with known ...
AbstractPGLa, a 21-residue member of the magainin family of antibiotic peptides, is shown to be heli...
AbstractUsing two-dimensional NMR spectroscopy, a complete 1H resonance assignment has been obtained...
AbstractThe membrane-active antimicrobial peptide PGLa from Xenopus laevis is known from solid-state...
AbstractTo gain further insight into the antimicrobial activities of cationic linear peptides, we in...
Magainin 2 and PGLa are cationic, amphipathic antimicrobial peptides which when added as equimolar m...
AbstractPGLa and magainin 2 (MAG2) are amphiphilic antimicrobial peptides from frog skin with known ...
AbstractPeptidyl-glycine-leucine-carboxyamide (PGLa), isolated from granular skin glands of Xenopus ...
AbstractThe structure and alignment of the amphipathic α-helical antimicrobial peptide PGLa in a lip...
Magainin 2 and PGLa are among the best-studied cationic antimicrobial peptides. They bind preferenti...