The major threat in modern medicine was biofilm forming bacterial related infections and they were highly tolerant to conventional antibiotics and a boundless demand for new drugs. In this regard, antimicrobial peptide (AMP) have been considered as potential alternative agents to conventional antibiotics. In this study, we have reported a CxxC zinc finger protein derived peptide, MF18 and its various biological role including activity against biofilm forming bacteria. Zinc finger protein are important in regulation of several cellular processes and wide range of molecular functions. The CxxC zinc finger protein identified from the cDNA library of a teleost fish; further it was characterised using various online bioinformatics programs. During the in-silico analysis, an AMP named MF18 was identified from the CxxC zinc finger protein, then it was synthesised for further biological activity studies. The antimicrobial activity of MF18 was confirmed against the biofilm clinical isolates such as Staphylococcus aureus and Escherichia coli. The MIC of the antimicrobial peptide at the concentration of 320 µM was observed against these two biofilm bacteria. The mechanism of the peptides was determined using bacteria on its membrane permeabilization ability by scanning electron microscopy. It is exhibited that the MF18 potentially influenced in damaging the morphology of the bacteria. The toxicity of MF18 against the continuous cell line (RAW 264.7) was demonstrated by MTT assay and also using peripheral red blood cells by haemolytic assay; both assays showed that the peptide have no toxicity on the cells at lower concentration. Overall, the study showed the potential therapeutic application of the peptide in pharma industry.

中文翻译：

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CxxC锌指蛋白衍生肽，MF18对抗生物膜形成。

现代医学的主要威胁是生物膜形成细菌相关的感染，它们对常规抗生素具有高度的耐受性，对新药的需求无穷。在这方面，抗菌肽（AMP）已被认为是常规抗生素的潜在替代药物。在这项研究中，我们报告了CxxC锌指蛋白衍生肽MF18及其各种生物学作用，包括对形成生物膜的细菌的活性。锌指蛋白在调节几种细胞过程和广泛的分子功能中很重要。从硬骨鱼的cDNA文库中鉴定出CxxC锌指蛋白；此外，使用各种在线生物信息学程序对其进行了表征。在计算机分析中，从CxxC锌指蛋白中鉴定出了名为MF18的AMP，然后将其合成用于进一步的生物学活性研究。证实MF18对生物膜临床分离株如金黄色葡萄球菌和大肠杆菌。观察到针对这两种生物膜细菌的抗菌肽的MIC为320 µM。使用细菌通过扫描电子显微镜确定其膜通透能力的机制。结果表明，MF18可能会破坏细菌的形态。通过MTT测定法证明了MF18对连续细胞系（RAW 264.7）的毒性，并且通过溶血测定法还使用了外周血红细胞。两种测定均表明该肽在较低浓度下对细胞无毒性。总的来说，该研究表明了该肽在制药工业中的潜在治疗应用。