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首页> 外文期刊>Biochemistry >The pi Configuration of the WWW Motif of a Short Trp-Rich Peptide Is Critical for Targeting Bacterial Membranes, Disrupting Preformed Biofilms, and Killing Methicillin-Resistant Staphylococcus aureus
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The pi Configuration of the WWW Motif of a Short Trp-Rich Peptide Is Critical for Targeting Bacterial Membranes, Disrupting Preformed Biofilms, and Killing Methicillin-Resistant Staphylococcus aureus

机译：富含TRP富含肽的WWW主题的PI配置对于靶向细菌膜是至关重要的，破坏预先形成的生物膜，并杀死耐甲氧西林金黄色葡萄球菌

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摘要

Tryptophan-rich peptides, being short and suitable for large-scale chemical synthesis, are attractive candidates for developing a new generation of antimicrobials to, combat antibiotic-resistant bacteria (superbugs). Although there are numerous pictures of the membrane bound structure of a single tryptophan (W), how multiple Trp amino acids assemble themselves and interact with bacterial membranes is poorly understood. This commuiiication presents the three-dimensional, structure of an eight-residue Tip-rich peptide (WWWLRKIW-NH2 with 50% deterthined by the improved two-dimensional nuclear magnetic resonance method, which includes the measurements of C-13 and N-15 chemical shifts at natural abundance. This peptide forms the shortest two-turn helix with a distinct amphipathic feature. A unique structural arrangement is identified for the Trp triplet, WWW, that forms a pi configuration with W2 as the horizontal bar and W-1/W-3 forming the two legs. An arginine scan reveals that the WWW motif is essential for killing methiciBin= resistant Staphylococcus,aureus USA300 and disrupting preformed bacterial hiofilms. This unique x configuration for the WWW motif is stabilized by aromatic aromatic, interactions as evidenced by ring current shifts as well as nuclear Overhauser effects. Because the WWW motif is maintained, a change of 17 to R led to a potent antimicrobial and antibiofilin peptide with 4-fold improvement in cell' selectivity. Collectively, this study elucidated' the structural basis of antibiofilm activity of the peptide, identified a better peptide candidate structure activity relationship studies, and laid the foundation for engineering future antibiotics based on the WWW motif.
机译：富含色氨酸的肽，短期且适合大规模化学合成，是制定新一代抗菌药物的有吸引力的候选者，用于打击抗生素抗性细菌（超前）。虽然单个色氨酸（W）的膜结合结构存在许多图片，但多个TRP氨基酸如何组装并与细菌膜相互作用是较差的。这种通告呈现了富含八残基脂肪的肽的三维结构（wwwlrkiw-nH2，通过改进的二维核磁共振方法与50％污染，包括C-13和N-15化学的测量在天然丰富的情况下转移。这种肽形成具有不同的两亲性特征的最短双转螺旋。为TRP三联网，WWW鉴定了独特的结构布置，其形成具有W2作为水平杆和W-1 / W的PI配置-3形成两条腿。精氨酸扫描表明，WWW主题对于杀死Methicibin =抗性葡萄球菌，金黄色葡萄球菌，AUREUS USA300并破坏预先形成的细菌HIOFILMS是必不可少的。这种独特的X配置通过芳香芳香族，相互作用稳定，稳定振铃电流换档以及核传承效应。由于维持了WWW图案，改变17至R导致有效的抗菌剂和抗生素肽，4倍细胞选择性的贪婪。本研究阐述了“肽的抗生素活性的结构基础，鉴定了更好的肽候选结构活性关系研究，并为基于WWW主题的工程未来抗生素奠定了基础。

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  • 来源
    《Biochemistry》 |2017年第31期|共5页
  • 作者

    Zarena D.; Mishra Biswajit; Lushnikoya Tamara; Wang Fangyu; Wang Guangshun;

  • 作者单位

    Univ Nebraska Med Ctr Dept Pathol &

    Microbiol Coll Med 986495 Nebraska Med Ctr Omaha NE 68198 USA;

    Univ Nebraska Med Ctr Dept Pathol &

    Microbiol Coll Med 986495 Nebraska Med Ctr Omaha NE 68198 USA;

    Univ Nebraska Med Ctr Dept Pathol &

    Microbiol Coll Med 986495 Nebraska Med Ctr Omaha NE 68198 USA;

    Univ Nebraska Med Ctr Dept Pathol &

    Microbiol Coll Med 986495 Nebraska Med Ctr Omaha NE 68198 USA;

    Univ Nebraska Med Ctr Dept Pathol &

    Microbiol Coll Med 986495 Nebraska Med Ctr Omaha NE 68198 USA;

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  • 正文语种 eng
  • 中图分类 生物化学;
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