title: Novel Hybrid Peptide Cecropin A (1-8)-LL37 (17-30) with Potential Antibacterial Activity.
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.
authors.affiliation: Laboratory of Feed Biotechnology, State Key Laboratory of Animal Nutrition, College of Animal Science and Technology, China Agricultural University, Beijing 100193, China. Weixubiao01@126.com.
authors.forename: Xu-Biao
authors.initials: XB
authors.lastname: Wei
authors.affiliation: Laboratory of Feed Biotechnology, State Key Laboratory of Animal Nutrition, College of Animal Science and Technology, China Agricultural University, Beijing 100193, China. lingxiabenpao@aliyun.com.
authors.forename: Ru-Juan
authors.initials: RJ
authors.lastname: Wu
authors.affiliation: Laboratory of Feed Biotechnology, State Key Laboratory of Animal Nutrition, College of Animal Science and Technology, China Agricultural University, Beijing 100193, China. lionsdy1@gmail.com.
authors.forename: Da-Yong
authors.initials: DY
authors.lastname: Si
authors.affiliation: Laboratory of Feed Biotechnology, State Key Laboratory of Animal Nutrition, College of Animal Science and Technology, China Agricultural University, Beijing 100193, China. liaoxd56@163.com.
authors.forename: Xiu-Dong
authors.initials: XD
authors.lastname: Liao
authors.affiliation: Laboratory of Feed Biotechnology, State Key Laboratory of Animal Nutrition, College of Animal Science and Technology, China Agricultural University, Beijing 100193, China. zhanglulu09@126.com.
authors.forename: Lu-Lu
authors.initials: LL
authors.lastname: Zhang
authors.affiliation: Laboratory of Feed Biotechnology, State Key Laboratory of Animal Nutrition, College of Animal Science and Technology, China Agricultural University, Beijing 100193, China. zhangrj621@126.com.
authors.forename: Ri-Jun
authors.initials: RJ
authors.lastname: Zhang
mesh_terms: D000818:Animals; D000900:Anti-Bacterial Agents / Q000009:adverse effects / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000009:adverse effects / Q000494:pharmacology*; D002701:Chloramphenicol / Q000009:adverse effects / Q000494:pharmacology; D004912:Erythrocytes / Q000187:drug effects; D004926:Escherichia coli / Q000187:drug effects; D006461:Hemolysis / Q000187:drug effects; D008855:Microscopy, Electron, Scanning; D009355:Neomycin / Q000009:adverse effects / Q000494:pharmacology; D012756:Sheep; D013211:Staphylococcus aureus / Q000187:drug effects; D013839:Thiamphenicol / Q000009:adverse effects / Q000494:pharmacology
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D002701:Chloramphenicol; C031161:cecropin A; D013839:Thiamphenicol; D009355:Neomycin
keywords: antibacterial activity; cecropin A (1–8)-LL37 (17–30); hemolytic activity; hybrid peptide; synergistic interaction