4.6 Article

The Lysozyme Inhibitor Thionine Acetate Is Also an Inhibitor of the Soluble Lytic Transglycosylase Slt35 from Escherichia coli

期刊

MOLECULES
卷 26, 期 14, 页码 -

出版社

MDPI
DOI: 10.3390/molecules26144189

关键词

lytic transglycosylase; thionine acetate; enzyme inhibition; antibacterial

资金

  1. UK Biotechnology and Biological Sciences Research Council (BBSRC) [BB/L01758X/1]
  2. Life Sciences Research NetworkWales [NRNRG4Mar039]
  3. Libyan Embassy (London) [10007]
  4. Royal Society of Chemistry, Undergraduate Research Bursary
  5. Cardiff University
  6. Swansea University
  7. BBSRC [BB/L01758X/1] Funding Source: UKRI

向作者/读者索取更多资源

Lytic transglycosylases like Slt35 are potential targets for novel antibacterial agents. Thionine acetate was found to be a weak inhibitor of both Slt35 and lysozyme, and also enhanced the efficacy of ampicillin against E. coli.
Lytic transglycosylases such as Slt35 from E. coli are enzymes involved in bacterial cell wall remodelling and recycling, which represent potential targets for novel antibacterial agents. Here, we investigated a series of known glycosidase inhibitors for their ability to inhibit Slt35. While glycosidase inhibitors such as 1-deoxynojirimycin, castanospermine, thiamet G and miglitol had no effect, the phenothiazinium dye thionine acetate was found to be a weak inhibitor. IC50 values and binding constants for thionine acetate were similar for Slt35 and the hen egg white lysozyme. Molecular docking simulations suggest that thionine binds to the active site of both Slt35 and lysozyme, although it does not make direct interactions with the side-chain of the catalytic Asp and Glu residues as might be expected based on other inhibitors. Thionine acetate also increased the potency of the beta-lactam antibiotic ampicillin against a laboratory strain of E. coli.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.6
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据