节点文献
氨曲南竞争性抑制NDM-1对β-内酰胺类抗生素的水解
Aztreonam Competitively Inhibits Hydrolysis of β-Lactam Antibiotics by NDM-1
【摘要】 文章以新德里金属-β-内酰胺酶1(NDM-1)为模型,研究在氨曲南存在的条件下,MBL对其它β-内酰胺类抗生素水解活性的影响。研究数据显示氨曲南能够显著抑制NDM-1对头孢硝噻吩或美罗培南的水解。用氨曲南处理固相于玻璃珠的NDM-1(NDM-1酶珠),结果显示处理后的NDM-1酶珠对青霉素G的水解活性有显著抑制,且即使经过多次充分冲洗,经氨曲南处理过的NDM-1酶珠对青霉素G的水解活性仍只是部分恢复,说明氨曲南与NDM-1酶具有强烈、稳定的结合活性,从而可有效竞争性抑制NDM-1酶对其他β-内酰胺类抗生素的水解。
【Abstract】 We investigated the effect of Aztreonam on hydrolysis of β-lactam antibiotics by MBL using New Delhi Metallo-β-lactamase-1(NDM-1) as a model. The results showed that Aztreonam significantly inhibited hydrolysis of Nitrocefin and Meropenem by soluble NDM-1, but also inhibited hydrolysis of Penicillin G by CPG beads immobilized NDM-1(NDM-1 beads). Moreover, in spite of extensive washing for multiple times, the activity to hydrolyze Penicillin G by the Aztreoman pre-treated NDM-1 beads was just partially recovered. These data suggest that Aztreonam can covalently and stably bind on NDM-1, thus efficiently inhibiting hydrolysis of other kinds of β-lactam antibiotics by NDM-1 in a competitive way.
【Key words】 aztreonam; NDM-1; metal-β-lactamase; superbug; antimicrobial resistance;
- 【文献出处】 山西大学学报(自然科学版) ,Journal of Shanxi University(Natural Science Edition) , 编辑部邮箱 ,2021年01期
- 【分类号】R978.1
- 【网络出版时间】2019-07-19 13:19
- 【被引频次】1
- 【下载频次】351