Fluorescence studies on the phase dependence of interactions between a tripeptide, lys-trp-lys, and dimyristoylphosphatidylserine.

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概要

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• Interactions of a basic tripeptide, lysyl-tryptophyl-lysine (LTL) with dimyristoylphosphatidylserine (DMPS) were investigated by fluorescence spectroscopy. An interacting LTL–DMPS complex assumes two distinctly different conformations in the lipid bilayer depending on the thermotropic phase of lipid. At temperatures below the gel–liquid crystalline phase-transition temperature (<I>T</I><SUB>c</SUB>), LTL binds to the polar head groups of DMPS through electrostatic force, and the tryptophan residue is located on the surface of the membrane because of the rigidity of the head groups. Above <I>T</I><SUB>c</SUB>, it assumes a conformation such that the tryptophan residue slips deeply into the DMPS bilayer. The temperature dependence of the fluorescence quenching by acrylamide supported the penetration of the tryptophan upon the phase transition of DMPS. A fluorescence decay analysis based on the photophysical deactivation mechanism of tryptophan residue has revealed a peculiar interaction of LTL with DMPS in the bilayer.

• 公益社団法人 日本化学会の論文

著者

• Yamashita Shoji

  Institute Of Biophysics Faculty Of Agriculture Graduate School Of Kyushu University

• Yamasaki Nobuyuki

  Laboratory Of Agricultural Process Engineering Faculty Of Agriculture Kyushu University

• Szabo Arthur

  Molecular Biochemistry, National Research Council Canada

• Krajcarski Donald

  Molecular Biochemistry, National Research Council Canada

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