(4-24)-ply(a) has been researched along with 1-palmitoyl-2-oleoylglycero-3-phosphoglycerol* in 2 studies
2 other study(ies) available for (4-24)-ply(a) and 1-palmitoyl-2-oleoylglycero-3-phosphoglycerol
| Article | Year |
|---|---|
Lipid saturation and head group composition have a pronounced influence on the membrane insertion equilibrium of amphipathic helical polypeptides.
The histidine-rich peptides of the LAH4 family were designed using cationic antimicrobial peptides such as magainin and PGLa as templates. The LAH4 amphipathic helical sequences exhibit a multitude of interesting biological properties such as antimicrobial activity, cell penetration of a large variety of cargo and lentiviral transduction enhancement. The parent peptide associates with lipid bilayers where it changes from an orientation along the membrane interface into a transmembrane configuration in a pH-dependent manner. Here we show that LAH4 adopts a transmembrane configuration in fully saturated DMPC membranes already at pHÂ 3.5, i.e. much below the pK Topics: Amino Acid Sequence; Antimicrobial Cationic Peptides; Dimyristoylphosphatidylcholine; Hydrogen-Ion Concentration; Hydrophobic and Hydrophilic Interactions; Lipid Bilayers; Magainins; Magnetic Resonance Spectroscopy; Phosphatidylcholines; Phosphatidylglycerols | 2022 |
Structure and dynamics of the antibiotic peptide PGLa in membranes by solution and solid-state nuclear magnetic resonance spectroscopy.
PGLa, a 21-residue member of the magainin family of antibiotic peptides, is shown to be helical between residues 6 and 21 when associated with detergent micelles by multidimensional solution nuclear magnetic resonance (NMR) spectroscopy. Solid-state NMR experiments on specifically 15N-labeled peptides in oriented phospholipid bilayer samples show that the helix axis is parallel to the plane of the bilayers. 15N solid-state NMR powder pattern line shapes obtained on unoriented samples demonstrate that the amino-terminal residues are highly mobile and that the fluctuations of backbone sites decrease from Ala6 toward the carboxy terminus. The powder pattern observed for 15N-labeled Ala20 is essentially that expected for a rigid site. These findings are similar to those for the 23-residue magainin2 peptide in membrane environments. Topics: Amino Acid Sequence; Antimicrobial Cationic Peptides; Lipid Bilayers; Micelles; Molecular Sequence Data; Nitrogen; Nuclear Magnetic Resonance, Biomolecular; Peptides; Phosphatidylethanolamines; Phosphatidylglycerols; Protein Conformation; Protein Structure, Secondary; Solutions | 1998 |