Design, Recombinant Expression, and Antibacterial Activity of the Cecropins-Melittin Hybrid Antimicrobial Peptides

被引：34

作者：

Cao, Yu ^{[1
]}

Yu, Rong Qing ^{[1
]}

Liu, Yi ^{[1
]}

Zhou, Huo Xiang ^{[1
]}

Song, Ling Ling ^{[1
]}

Cao, Yi ^{[1
]}

Qiao, Dai Rong ^{[1
]}

机构：

[1] Sichuan Univ, Coll Life Sci, Microbiol & Metab Engn Key Lab Sichuan Prov, Chengdu 610064, Sichuan, Peoples R China

来源：

CURRENT MICROBIOLOGY | 2010年 / 61卷 / 03期

基金：

中国国家自然科学基金;

关键词：

INNATE IMMUNITY; MOLECULAR-BASIS; MEMBRANE; ANTIBIOTICS; MECHANISMS; SKIN;

D O I：

10.1007/s00284-010-9592-7

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

In order to evaluate their antibacterial activities and toxicities, the cecropins-melittin hybrid antimicrobial peptide, CA(1-7)-M(4-11) (CAM) and CB(1-7)-M(4-11) (CBM), were designed by APD2 database. The recombinant hybrid antimicrobial peptides were successfully expressed and purified in Pichia pastoris. Antimicrobial activity assay showed that both of the two hybrid antimicrobial peptides had strong antibacterial abilities against Escherichia coli, Staphylococcus aureus, Pseudomonas aeruginosa, Klebsiella pneumoniae, Bacillus subtilis, Bacillus thuringiensis, and Salmonella derby. The potency of CAM and CBM to E. coli 25922 were 0.862 and 0.849, respectively, slightly lower than Amp's 0.957. The hemolytic assays indicated CAM and CBM had no hemolytic in vivo and in vitro, and so they had a good application prospect.

引用

页码：169 / 175

页数：7

共 24 条

[1] SHORTENED CECROPIN-A MELITTIN HYBRIDS - SIGNIFICANT SIZE-REDUCTION RETAINS POTENT ANTIBIOTIC-ACTIVITY [J].