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具有潜在抗菌活性的新型杂合肽天蚕素A(1-8)-LL37(17-30)

Novel Hybrid Peptide Cecropin A (1-8)-LL37 (17-30) with Potential Antibacterial Activity.

作者信息

Wei Xu-Biao, Wu Ru-Juan, Si Da-Yong, Liao Xiu-Dong, Zhang Lu-Lu, Zhang Ri-Jun

机构信息

Laboratory of Feed Biotechnology, State Key Laboratory of Animal Nutrition, College of Animal Science and Technology, China Agricultural University, Beijing 100193, China.

出版信息

Int J Mol Sci. 2016 Jun 29;17(7):983. doi: 10.3390/ijms17070983.

Abstract

Hybridizing different antimicrobial peptides (AMPs) is a particularly successful approach to obtain novel AMPs with increased antimicrobial activity but minimized cytotoxicity. The hybrid peptide cecropin A (1-8)-LL37 (17-30) (C-L) combining the hydrophobic N-terminal fragment of cecropin A (C) with the core antimicrobial fragment of LL37 (L) was designed and synthesized. C-L showed higher antibacterial activity against all indicator strains than C and L, and no hemolytic activity to sheep erythrocytes was observed. C-L kills bacterial cells and causes disruption of surface structure, as determined by scanning electron microscopy. Synergistic effects were observed in the combination of C-L with several antibiotics (chloramphenicol, thiamphenicol, or neomycin sulfate) against Escherichia coli and Staphylococcus aureus.

摘要

杂交不同的抗菌肽(AMPs)是获得具有增强抗菌活性但细胞毒性最小化的新型抗菌肽的一种特别成功的方法。设计并合成了将天蚕素A(C)的疏水性N端片段与LL37(L)的核心抗菌片段相结合的杂交肽天蚕素A(1-8)-LL37(17-30)(C-L)。C-L对所有指示菌株的抗菌活性均高于C和L,并且未观察到对绵羊红细胞的溶血活性。通过扫描电子显微镜确定,C-L可杀死细菌细胞并导致表面结构破坏。在C-L与几种抗生素(氯霉素、甲砜霉素或硫酸新霉素)联合使用时,对大肠杆菌和金黄色葡萄球菌具有协同作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9d1a/4964367/4471a2368b2b/ijms-17-00983-g001.jpg

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