Investigation of the sequence and length dependence for cell-penetrating prenylated peptides

被引：12

作者：

Wollack, James W. ^{[1
]}

Zeliadt, Nicholette A. ^{[2
]}

Ochocki, Joshua D. ^{[1
]}

Mullen, Daniel G. ^{[1
]}

Barany, George ^{[1
]}

Wattenberg, Elizabeth V. ^{[2
]}

Distefano, Mark D. ^{[1
]}

机构：

[1] Univ Minnesota, Dept Chem, Minneapolis, MN 55455 USA

[2] Univ Minnesota, Div Environm Hlth Sci, Minneapolis, MN 55455 USA

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2010年 / 20卷 / 01期

基金：

美国国家卫生研究院;

关键词：

Cell-penetrating peptide; Prenylataion; Lipid modification; Geranylgeranyl; Posttranslational modification; Prenylated peptide; PROTEIN PRENYLATION; MEMBRANE; GENES;

D O I：

10.1016/j.bmcl.2009.11.026

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

Cell penetrating peptides are useful delivery tools for introducing molecules of interest into cells. A new class of cell penetrating molecules has been recently reported-cell penetrating, prenylated peptides. In this study a series of such peptides was synthesized to examine the relationship between peptide sequence and level of peptide internalization and to probe their mechanism of internalization. This study revealed that prenylated peptides internalize via a non-endocytotic pathway regardless of sequence. Sequence length and identity was found to play a role in peptide uptake but prenylated sequences as short as two amino acids were found to exhibit significant cell penetrating properties. (C) 2009 Elsevier Ltd. All rights reserved.

引用

页码：161 / 163

页数：3

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