Interaction of a hydrophobic model peptide and its fatty acid derivative with lipid vesicles

FEBS Letters

Joseph, M.¹  Nagaraj, R.¹ 

[1] Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, India

关键词: Hydrophobic peptide;    Fatty acid acylation;    Fluorescence spectroscopy;    Fluorescence quenching;   

DOI  :  10.1016/0014-5793(88)80522-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The interaction of a peptide [Lys-Phe-Phe-Phe-Ile-Ile-Trp-OCH₃] and its fatty acid derivatives [Lys-(ε-palmitoyl)-Phe-Phe-Phe-Ile-Ile-Trp-OCH₃ and Lys-{ε-12-(9-anthroyloxy)stearic acid}-Phe-Phe-Phe-Ile-Ile-OCH₃] with model membranes was investigated by fluorescence spectroscopy. The emission characteristics of the Trp fluorophore indicated that only the peptide with the fatty acid chain is associated with lipid vesicles. Quenching experiments with spin probes suggest an orientation for the fatty acylated peptide wherein the fatty acid chain is perpendicular to the bilayer surface and the peptide chain parallel to the bilayer surface.

【 授权许可】

Unknown