
Interactions of the insect neuropeptide proctolin (Arg-Tyr-Leu-Pro-Thr), its [beta-cyclohexyl-(4-O-methyl)2]-L-alanine analog, and the leucopyrokinin [2-8]-fragment (Thr-Ser-Phe-Thr-Pro-Arg-Leu-NH2), with synthetic phospholipids (DPPC, DMPE, DMPG) were studied using the microcalorimetric method. Most pronounced changes of the lipid thermotropic behavior were observed with DMPG/leucopyrokinin [2-8]-fragment mixtures. Proctolin itself was less active with all the lipids studied. The results obtained suggest that the studied peptides interact with the head group region of lipid bilayer.
Insecta, Lipid Bilayers, Molecular Sequence Data, Neuropeptides, Calorimetry, Peptide Fragments, Pyrrolidonecarboxylic Acid, Insect Hormones, Animals, Amino Acid Sequence, Oligopeptides, Phospholipids
Insecta, Lipid Bilayers, Molecular Sequence Data, Neuropeptides, Calorimetry, Peptide Fragments, Pyrrolidonecarboxylic Acid, Insect Hormones, Animals, Amino Acid Sequence, Oligopeptides, Phospholipids
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