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首页> 外文期刊>International Journal of Peptide Research and Therapeutics >The Proline-rich Antibacterial Peptide Bac7 Binds to and Inhibits in vitro the Molecular Chaperone DnaK
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The Proline-rich Antibacterial Peptide Bac7 Binds to and Inhibits in vitro the Molecular Chaperone DnaK

机译：富含脯氨酸的抗菌肽Bac7结合并在体外抑制分子伴侣DnaK。

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摘要

Bac7, a cathelicidin peptide of the proline-rich group, inactivates bacteria in a stereospecific manner by entering target cells without any apparent membrane damage and by binding to as yet unknown intracellular targets. The present study was aimed at detecting these putative intracellular interactors, which might mediate the antibacterial action of this peptide. By using affinity resins functionalized with the N-terminal 1-35 fragment of Bac7, a single protein was specifically retained with high affinity from Escherichia coli cytoplasmic protein lysates. This ligand was identified as the heat shock protein DnaK, the Hsp70 homolog in E. coli. The interaction between the peptide and the chaperone is stereospecific, given that a resin prepared with the all- d enantiomer failed to retain the protein. In vitro, Bac7(1-35) formed a complex with DnaK with an affinity comparable to that of other known high-affinity peptide ligands. In addition, at 10–100 μM concentration, the peptide inhibited the protein refolding activity of the complete DnaK/DnaJ/GrpE/ATP molecular chaperone system in a dose-dependent manner. Despite these results, the in vitro sensitivity to the peptide, under growth permitting conditions, of DnaK-deficient E. coli strains was not significantly affected compared to the wild-type strain. This suggests that, apart from DnaK, other vital targets for the proline-rich AMPs are present in susceptible bacteria.
机译：Bac7是富含脯氨酸的基团中的cathelicidin肽，可通过进入靶细胞而没有任何明显的膜损伤，并结合至今尚未知的细胞内靶，以立体特异性方式灭活细菌。本研究旨在检测可能介导该肽的抗菌作用的这些假定的细胞内相互作用物。通过使用用Bac7的N末端1-35片段功能化的亲和树脂，可以从大肠杆菌胞质蛋白裂解物中以高亲和力特异性保留单个蛋白。该配体被鉴定为热激蛋白DnaK，E.coli中的Hsp70同源物。考虑到用全对映异构体制备的树脂无法保留蛋白质，因此肽与分子伴侣之间的相互作用具有立体特异性。在体外，Bac7（1-35）与DnaK形成复合物，其亲和力可与其他已知的高亲和力肽配体相媲美。此外，在10-100μM的浓度下，该肽以剂量依赖的方式抑制了整个DnaK / DnaJ / GrpE / ATP分子伴侣系统的蛋白质重折叠活性。尽管有这些结果，与野生型菌株相比，在生长允许的条件下，缺乏DnaK的大肠杆菌菌株对肽的体外敏感性没有受到显着影响。这表明，除了DnaK之外，易感细菌中还存在富含脯氨酸的AMPs的其他重要靶标。

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