首页> 外文期刊>Canadian Journal of Pure and Applied Sciences >HETEROLOGOUS PRODUCTION OF SYNTHETIC CATIONIC ANTIMICROBIAL PEPTIDE IN NOVEL OSMOTICALLY INDUCIBLE E.COLI GJ1158
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HETEROLOGOUS PRODUCTION OF SYNTHETIC CATIONIC ANTIMICROBIAL PEPTIDE IN NOVEL OSMOTICALLY INDUCIBLE E.COLI GJ1158

机译:新型渗透诱导大肠杆菌GJ1158的合成阳离子型抗菌肽的异源生产

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Cationic antimicrobial peptides are the upcoming therapeutic molecules as alternative drugs to the antibiotics. These peptides have a good scope in current antibiotic research. In the present study E. coli strain GJ1158 host was chosen for the expression of gene for Insilco designed synthetic peptide, Using Modified M9 medium. Various trails were carried out to optimize the recombinant peptide production in modified M9 medium by following the Placket Burman model. The optimal media was chosen for further expression studies and the expressed antimicrobial peptide was purified using Immobilized Metal Affinity Chromatography (IMAC) system. The product was visualized on 16% Tricine SDS-PAGE. It was identified that 30% of the bacterial proteins as the recombinant protein. The expressed antimicrobial peptide was purified using Immobilized Metal Affinity Chromatography (IMAC) system. The antimicrobial activity of purified peptide using Top agar assay showed that the recombinant antimicrobial peptide has high antibacterial activity against both Gram-positive and -negative bacteria.
机译:阳离子抗菌肽是即将出现的治疗分子,可作为抗生素的替代药物。这些肽在当前的抗生素研究中具有很好的范围。在本研究中,使用改良的M9培养基,选择了大肠杆菌菌株GJ1158宿主来表达Insilco设计的合成肽的基因。通过遵循Placket Burman模型,进行了各种试验以优化在修饰的M9培养基中的重组肽产生。选择最佳培养基进行进一步的表达研究,并使用固定化金属亲和层析(IMAC)系统纯化表达的抗菌肽。产物在16%Tricine SDS-PAGE上可视化。鉴定出30%的细菌蛋白为重组蛋白。使用固定化金属亲和色谱(IMAC)系统纯化表达的抗菌肽。使用Top琼脂测定法纯化的肽的抗菌活性表明,该重组抗菌肽对革兰氏阳性和阴性细菌均具有高抗菌活性。

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