Characterization of Novel Antimicrobial Peptides from the Epidermis of Clarias batrachus Catfish

IF 4.6 Q2 MATERIALS SCIENCE, BIOMATERIALS ACS Applied Bio Materials Pub Date : 2024-02-03 DOI:10.1007/s10989-024-10589-8

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Abstract

In this study, an antimicrobial protein (AMP) from the epidermis of catfish (Clarias batrachus) was purified and characterized for its molecular and antimicrobial properties. The crude epidermal extract was subjected to precipitation of proteins using 70% ammonium sulphate saturation followed by dialysis and protein separation by reverse phase ultra fast liquid chromotography (UFLC) using the C₁₈ column. The active peptides obtained from fractions 1, 2, and 3 were screened for antimicrobial activity against different bacterial pathogens with a minimum 5 mg/ml inhibitory concentration. An active fraction with a retention time (RT) of 27.069 from the UFLC chromatogram exhibited significant antimicrobial activity against broad-spectrum bacterial and fungal organisms, including multidrug-resistant clinical isolates. The RT 27.069, identified as cationic AMP of fraction-3, has a molecular weight of 25 kDa as determined by MALDI-TOF mass spectrometry. Further studies by Mascot search and BLAST analysis using the partial sequence of AMP showed that the protein has high homologs to pleurocidin-like peptide (Plp) from a fish Pleuronectus americanus. Moreover, the identified AMP is a cationic peptide with a good stability index, having a score of 31.50 predicted by the ProtParam. Therefore, the identified antimicrobial peptide (Plp) indicates that this cost-effective natural substance obtained from fish could potentially be used as a treatment for several bacterial and fungal infections in humans.

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蝠鲼鲶鱼表皮中新型抗菌肽的表征

摘要本研究从鲶鱼（Claras batrachus）表皮中纯化了一种抗菌蛋白（AMP），并对其分子和抗菌特性进行了表征。表皮粗提取物经 70% 硫酸铵饱和沉淀后进行透析，然后使用 C18 柱通过反相超快液相色谱法（UFLC）分离蛋白质。对从馏分 1、2 和 3 中获得的活性肽进行了筛选，以检测其对不同细菌病原体的抗菌活性，最小抑菌浓度为 5 毫克/毫升。在 UFLC 色谱图中，保留时间（RT）为 27.069 的活性馏分对广谱细菌和真菌（包括耐多药的临床分离株）具有显著的抗菌活性。经 MALDI-TOF 质谱测定，RT 27.069 被确定为馏分-3 中的阳离子 AMP，分子量为 25 kDa。利用 AMP 的部分序列进行的 Mascot 搜索和 BLAST 分析表明，该蛋白与来自美洲褶鱼的褶菌素样肽（Plp）具有高度同源性。此外，鉴定出的 AMP 是一种阳离子肽，具有良好的稳定性指数，ProtParam 预测得分为 31.50。因此，鉴定出的抗菌肽（Plp）表明，这种从鱼类中获得的具有成本效益的天然物质可用于治疗人类的多种细菌和真菌感染。

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