A dimerization "switch" in the internalization mechanism of a cell-penetrating peptide

被引：13
|
作者：
Moss, JA
Lillo, A
Kim, YS
Gao, CS
Ditzel, H
Janda, KD
机构：
[1] Scripps Res Inst, Dept Chem, La Jolla, CA 92037 USA
[2] Scripps Res Inst, Dept Immunol, La Jolla, CA 92037 USA
[3] Skaggs Inst Chem Biol, La Jolla, CA 92037 USA
来源：
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2005年 / 127卷 / 02期
关键词：
D O I：
10.1021/ja0443171
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
The internalization mechanism of a cell-penetrating peptide has been explored through combinatorial selection of a phage-displayed peptide dimer library, chemical synthesis, and biophysical characterization. Both energy-dependent and energy-independent modes for peptide uptake by the target mammalian cells were observed, suggesting a role for higher-order structure in modulating the action of this novel cell-penetrating peptide. Copyright © 2005 American Chemical Society.
引用
收藏
页码：538 / 539
页数：2
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