Peptide fragment hybridization is an effective method to obtain novel hybrid antimicrobial peptides with higher antibacterial activities. The novel peptide, valine-cecropin A(1–8)-plantaricin ZJ5(1–18) (CA-P), was designed by coupling the amphiphilic N-terminal fragment of CA with the N-terminal core helix of P and adding a valine residue to the N-terminus of the hybrid fragment. CA-P showed higher antibacterial activities than the parental peptide P against all indicator strains in the experiment, with no hemolytic activity against sheep red blood cells. Observations by scanning electron microscopy and transmission electron microscopy confirmed that CA-P destroyed the surface structure of the bacteria and caused leakage of the cellular contents. As determined by fluorescence microscopy, the antibacterial mechanism of CA-P is microorganism killing. It was observed that CA-P and Litsea mollis Hemsl. essential oil showed a significant synergistic effect against Salmonella enterica serovar Newport.

肽片段杂交是获得具有较高抗菌活性的新型杂合抗菌肽的有效方法。通过将CA的两亲性N末端片段与P的N末端核心螺旋偶联并添加，设计出新型肽，缬氨酸-天蚕素A（1-8）-车瑞霉素ZJ5（1-18）（CA-P）杂合片段N末端的缬氨酸残基。在实验中，CA-P对所有指示菌株均显示出比亲本肽P高的抗菌活性，对绵羊红细胞没有溶血活性。通过扫描电子显微镜和透射电子显微镜的观察证实，CA-P破坏了细菌的表面结构并引起细胞内容物的泄漏。如通过荧光显微镜所确定的，CA-P的抗菌机制是杀灭微生物。Litsea mollis Hemsl。精油对肠沙门氏菌纽波特沙门氏菌具有显着的协同作用。