您好，欢迎访问河南省农业科学院 机构知识库！
河南省农业科学院机构知识库

全部

  • 全部
  • 标题
  • 学者
  • 机构
  • 关键词

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

文献类型： 外文期刊

作者： Zarena, D. 1 ; Mishra, Biswajit 1 ; Lushnikoya, Tamara 1 ; Wang, Fangyu 1 ; Wang, Guangshun 1 ;

作者机构： 1.Univ Nebraska Med Ctr, Dept Pathol & Microbiol, Coll Med, 986495 Nebraska Med Ctr, Omaha, NE 68198 USA

2.JNTUA Coll Engn, Dept Phys, Anantapur 515002, Andhra Pradesh, India

3.Henan Acad Agr Sci, Henan Key Lab Anim Immunol, Zhengzhou 450002, Henan, Peoples R China

期刊名称：BIOCHEMISTRY （ 影响因子：3.162； 五年影响因子：3.045 ）

ISSN：

年卷期：

页码：

收录情况： SCI

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.

  • 相关文献
作者其他论文 更多>>
置顶
购物车
反馈

© 京ICP备09089781号-29 主办单位：河南省农业科学院

学术资源： 中国农业科学院 农业专业知识服务系统 农科联盟资源共建共享平台 中国农业科技文献与信息服务平台 中国农业期刊集成服务平台