Substrate optimization for monitoring cathepsin C activity in live cells

被引：17
|
作者：
Li, Jun [1 ]
Petrassi, H. Michael [1 ]
Tumanut, Christine [1 ]
Masick, Brian T. [1 ]
Trussell, Christopher [1 ]
Harris, Jennifer L. [1 ]
机构：
[1] Novartis Res Fdn, Genom Inst, San Diego, CA 92121 USA
来源：
BIOORGANIC & MEDICINAL CHEMISTRY | 2009年 / 17卷 / 03期
关键词：
Cathepsin; Imaging; Rhodamine; Activity-based probe; DIPEPTIDYL-PEPTIDASE-I; SERINE PROTEASES; ACTIVATION; MUTATIONS; ARTHRITIS;
D O I：
10.1016/j.bmc.2008.02.002
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：
A series of peptidic fluorogenic substrates were synthesized to develop a flow cytometry assay (FACS) to monitor the proteolytic activity of cathepsin C in live cells. Of the 16 substrates tested, (NH2-aminobutyric-homophenylalanine)(2)-rhodamine demonstrated the best reactivity and selectivity profile in the FACS assay using the B721 human B-lymphoblastoid cell line. The resulting FACS assay was validated through correlation of the IC50 values with a competitive radiolabeling assay against a series of small molecule inhibitors of cathepsin C. (C) 2008 Elsevier Ltd. All rights reserved.
引用
收藏
页码：1064 / 1070
页数：7
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