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Structure and Function of a Potent Lipopolysaccharide-Binding Antimicrobial and Anti-inflammatory Peptide
文献类型:期刊论文
作者 | Wei L1; Yang JJ2; He XQ1; Mo GX1; Hong J4; Yan XW[*]1; Lin DH[*]2; Lai R[*]1,3 |
刊名 | JOURNAL OF MEDICINAL CHEMISTRY
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出版日期 | 2013 |
卷号 | 56期号:9页码:3546-3556 |
通讯作者 | yanxw@njau.edu.cn ; dhlin@xmu.edu.cn ; rlai72@njau.edu.cn |
合作状况 | 其它 |
英文摘要 | Antimicrobial peptides (AMPs) play pivotal roles in the innate defense of vertebrates. A novel AMP (cathelicidin-PY) has been identified from the skin secretions of the frog Paa yunnanensis. Cathelicidin-PY has an amino acid sequence of RKCNFLCICLICEICLRTVITSHIDKVLRPQG. Nuclear magnetic resonance (NMR) spectroscopy analysis revealed that cathelicidin-PY adopts a tertiary structure with a mostly positively charged surface containing a helix (Thr15-Ser19). It possesses strong antimicrobial activity, low hemolytic activity, low cytotoxicity against RAW 264.7 cells, and strong anti-inflammatory activity. The action of antimicrobial activity of cathelicidin-PY is through the destruction of the cell membrane. Moreover, cathelicidin-PY exerts anti-inflammatory activity by inhibiting the production of nitric oxide (NO) and inflammatory cytokines such as tumor necrosis factor (TNF-alpha), interleukin-6 (IL-6), and monocyte chemoattractant protein-1 (MCP-1). Cathelicidin-PY inhibits the activation of Toll-like receptor 4 (TLR4) inflammatory response pathways induced by lipopolysaccharide (LPS). The NMR titration experiments indicated that cathelicidin-PY can bind to LPS. In conclusion, we have identified a novel potent peptide antibiotic with both antimicrobial and anti-inflammatory activities and laid the groundwork for future research and development. |
收录类别 | SCI |
资助信息 | This work was supported by Chinese National Natural Science Foundation (30830021, 31025025, 31070701, 31000960, 31025025, U1132601, 31000335, 31170717), the Ministry of Science and Technology (2010CB529800, 2009ZX09103-1/091, 2011ZX09102-002- 10), the Ministry of Agriculture (2009ZX08009-159B), Jiangsu Province (BK2012365 and BE2012748), Yunnan Province Y103951111, and Nanjing Agricultural University (KJ2012023). |
语种 | 英语 |
WOS记录号 | WOS:000318892500011 |
公开日期 | 2013-06-21 |
源URL | [http://159.226.149.42:8088/handle/152453/7508] ![]() |
专题 | 昆明动物研究所_动物毒素室 昆明动物研究所_动物模型与人类重大疾病机理重点实验室 |
作者单位 | 1.Life Sciences College of Nanjing Agricultural University, Nanjing 210095, Jiangsu, China 2.Key Laboratory of Chemical Biology of Fujian Province, Department of Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, Fujian, China 3.Key Laboratory of Animal Models and Human Disease Mechanisms, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, Yunnan, China 4.College of Biological Science and Technology, Fuzhou University, Fuzhou 380108, Fujian, China |
推荐引用方式 GB/T 7714 | Wei L,Yang JJ,He XQ,et al. Structure and Function of a Potent Lipopolysaccharide-Binding Antimicrobial and Anti-inflammatory Peptide[J]. JOURNAL OF MEDICINAL CHEMISTRY,2013,56(9):3546-3556. |
APA | Wei L.,Yang JJ.,He XQ.,Mo GX.,Hong J.,...&Lai R[*].(2013).Structure and Function of a Potent Lipopolysaccharide-Binding Antimicrobial and Anti-inflammatory Peptide.JOURNAL OF MEDICINAL CHEMISTRY,56(9),3546-3556. |
MLA | Wei L,et al."Structure and Function of a Potent Lipopolysaccharide-Binding Antimicrobial and Anti-inflammatory Peptide".JOURNAL OF MEDICINAL CHEMISTRY 56.9(2013):3546-3556. |
入库方式: OAI收割
来源:昆明动物研究所
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