Enzyme-Activatable Cell-Penetrating Peptides through a Minimal Side Chain Modification

被引：24

作者：

Bode, Saskia A. ^{[1
]}

Hansen, Morten B. ^{[1
]}

Oerlemans, Roy A. J. F. ^{[1
]}

van Hest, Jan C. M. ^{[1
]}

Lowik, Dennis W. P. M. ^{[1
]}

机构：

[1] Radboud Univ Nijmegen, Inst Mol & Mat, Bioorgan Chem, NL-6525 AJ Nijmegen, Netherlands

来源：

BIOCONJUGATE CHEMISTRY | 2015年 / 26卷 / 05期

关键词：

HUMAN AMINOPEPTIDASE-N; IN-VIVO; DELIVERY; DRUG; CD13; MOLECULES; MECHANISM; RECEPTOR; DESIGN; TARGET;

D O I：

10.1021/acs.bioconjchem.5b00066

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Activatable cell-penetrating peptides are of great interest in drug delivery because of their enhanced selectivity which can be controlled by the external stimuli that trigger their activation. The use of a specific enzymatic reaction to trigger uptake of an inert peptide offers a relevant targeting strategy because the activation process takes place a short time and only in areas where the specific cell surface enzyme is present. To this aim, the lysine side chain of Tat peptides was modified with an enzyme-cleavable domain of minimal size. This yielded blocked Tat-peptides which were inactive but that could be activated by coincubation with the selected enzymes.

引用

页码：850 / 856

页数：7

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