Interaction of gramicidin S analogs with lipid bilayer membrane.
One of the side chains of Orn residues in gramicidin S (GS) was connected with alanine (AGS), sarcosine (SGS), or histidine (HGS) residue, aiming at developing membrane-active artificial enzymes by virtue of the membrane-associating property of GS. The conformation of the GS analogs was similar to that of GS. However, the affinity of GS and its analogs for dipalmitoylphosphatidylcholine (DPPC) vesicles decreased in the order of GS greater than SGS greater than HGS congruent to AGS. The addition of GS analogs at 10 microM to DPPC vesicles decreased the membrane fluidity, indicating that GS analogs did not disrupt the vesicular structure of DPPC vesicles. On the other hand, GS analogs enhanced carboxyfluorescein-leakage from DPPC vesicles. It was therefore considered that the GS analogs induced the phase-separation of the lipid bilayer membrane. Hydrolytic reactions of HGS in the presence of DPPC vesicles were studied using N-methylindoxyl alkanoate as substrate. HGS reacted only with N-methylindoxyl hexanoate below the phase-transition temperature of the membrane. The substrate specificity of HGS was ascribed to the condensation of HGS in the neighbourhood of the substrate in the lipid bilayer membrane due to the phase-separation below the phase-transition temperature of the membrane.
Yagi
Y
Y
Department of Polymer Chemistry, Kyoto University, Japan.
Kimura
S
S
Imanishi
Y
Y
D015060:1,2-Dipalmitoylphosphatidylcholine / Q000378:metabolism; D000595:Amino Acid Sequence; D002384:Catalysis; D004952:Esters; D006096:Gramicidin / Q000138:chemical synthesis / Q000378:metabolism*; D006868:Hydrolysis; D008051:Lipid Bilayers / Q000378:metabolism*; D008081:Liposomes; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013499:Surface Properties
D004952:Esters; D008051:Lipid Bilayers; D008081:Liposomes; D006096:Gramicidin; D015060:1,2-Dipalmitoylphosphatidylcholine