Colorimetric sensing strategy for β-lactamase inhibitor using generation of 2-amino-3-mercapto-3-methylbutanoic acid via enzyme catalysis and Cu(II)-mediated redox

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• 作者：Jun Lv^a ; ^bAuthor Vitae ; Chen Chen^bAuthor Vitae ; Chao Qian^bAuthor Vitae ; Wanyi Chen^aAuthor Vitae ; Yang Xiang^c ; ^{xiangy@nju.edu.cn" class="auth_mail" title="E-mail the corresponding author}Author Vitae ; Juan Zhang^a ; ^b ; ^{juanzhang@shu.edu.cn" class="auth_mail" title="E-mail the corresponding author}Author Vitae
• 关键词：Colorimetric method ; β-Lactamase ; Inhibitor ; 2-Amino-3-mercapto-3-methylbutanoic acid ; Cu(II)-mediated redox
• 刊名：Sensors & Actuators: B. Chemical
• 出版年：2016
• 出版时间：July 2016
• 年：2016
• 卷：230
• 期：Complete
• 页码：653-657
• 全文大小：1107 K

文摘

A colorimetric sensing method has been proposed for the detection of β-lactamase (β-Lac) activity and the screening of the inhibitors in this work. The method is based on the aggregation of AuNPs induced by 2-amino-3-mercapto-3-methylbutanoic acid (AMMBA) through the formation of Au-S bond and electrostatic interaction. Since AMMBA can form through β-Lac catalyzed hydrolysis and Cu(II)-mediated redox with penicillin as enzyme substrate, β-Lac activity is related to the extent of AuNPs aggregation. The enzyme activity can be determined at levels as low as 0.556 U/mL and over a linear detection range as wide as from 0 U/mL to 30 U/mL. Furthermore, the inhibitory effects of clavulanic acid and sulbactam on the activity of β-Lac have also been tested and given IC₅₀ values of 0.92 μM and 0.06 μM, respectively. The proposed method can be not only used for the detection of β-Lac activity but also the screening of the inhibitor.