Eliminating caspase-7 and cathepsin B cross-reactivity on fluorogenic caspase-3 substrates

被引：3
|
作者：
Mackay, Martha [1 ]
Perez-Lopez, Ana M. [1 ]
Bradley, Mark [1 ]
Lilienkampf, Annamaria [1 ]
机构：
[1] Univ Edinburgh, Sch Chem, EaStCHEM, W Mains Rd, Edinburgh EH9 3FJ, Midlothian, Scotland
来源：
MOLECULAR BIOSYSTEMS | 2016年 / 12卷 / 03期
基金：
英国工程与自然科学研究理事会;
关键词：
ACTIVITY-BASED PROBES; RESONANCE ENERGY-TRANSFER; UNNATURAL AMINO-ACIDS; APOPTOTIC CELL-DEATH; FLUORESCENT PEPTIDE; LIVE CELLS; FAMILY PROTEASES; INHIBITORS; ACTIVATION; IDENTIFICATION;
D O I：
10.1039/c5mb00730e
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：
11 FRET-based fluorogenic substrates were constructed using the pentapeptide template Asp-Glu-X-2-Asp-X-1', and evaluated with caspase-3, caspase-7 and cathepsin B. The sequence Asp-Glu-Pro-Asp-Ser was able to selectively quantify caspase-3 activity in vitro without notable caspase-7 and cathepsin B cross-reactivity, while exhibiting low mu M KM values and good catalytic efficiencies (7.0-16.9 mu M-1 min(-1)).
引用
收藏
页码：693 / 696
页数：4
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