NMR solution structure and position of transportan in neutral phospholipid bicelles

被引:63
作者
Bárány-Wallje, E [1 ]
Andersson, A [1 ]
Gräslund, A [1 ]
Mäler, L [1 ]
机构
[1] Univ Stockholm, Arrhenius Lab, Dept Biochem & Biophys, S-10691 Stockholm, Sweden
来源
FEBS LETTERS | 2004年 / 567卷 / 2-3期
关键词
cell-penetrating peptide; transportan; NMR; solution structure; bicelle;
D O I
10.1016/j.febslet.2004.04.079
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Transportan is a chimeric cell-penetrating peptide constructed from the peptides galanin and mastoparan, which has the ability to internalize living cells carrying a hydrophilic load. In this study, we have determined the NMR solution structure and investigated the position of transportan in neutral bicelles. The structure revealed a well-defined -helix in the C-terminal mastoparan part of the peptide anti a weaker tendency to form an -helix in the N-terminal domain. The position of the peptide in relation to the membrane, as studied by adding paramagnetic probes, shows that the peptide lies parallel to, and in the head-group region of the membrane surface. This result is supported by amide proton secondary chemical shifts. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:265 / 269
页数:5
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