Preferential interaction of pentagastrin with the gel state of dimyristoyl glycerophosphocholine
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Fluorescence and circular dichroism spectra indicate that pentagastrin interacts with dimyristoyl glycerophosphocholine more strongly below the phase transition temperature of the lipid than above it. Studies on the interaction of several peptides with dimyristoyl glycerophosphocholine suggest that this property may be related to the ability of these peptides to form amphipathic structures containing two hydrophobic amino acids separated by two other amino acids. Pentagastrin has a marked effect on the proton magnetic resonance spectra of dipalmitoyl glycerophosphocholine below the phase transition temperature indicating the the peptide decreases the motional freedom of the lipid.
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