Bioinformatics Analysis of Fish-Derived β-Defensin
Fish-derived β-defensin is an important member of the antimicrobial peptide family.It has the characteristics of broad-spectrum antibacterial,does not damage eukaryotic cells,and is not easy to express drug resistance.It can be applied to fishery breeding,human clinical and other aspects.Nevertheless,it now faces issues with a difficult extraction procedure,poor yield,high manufacturing costs,and a high demand for the proteases needed for the extraction.Thus,it is crucial to examine its physicochemical characteristics,structure,and bactericidal action as well as to create practical and affordable derived peptides.In this study,the physicochemical properties,secondary structure,phosphorylation and glycosylation sites,hydrophobicity,intracellular localization and signal peptide were predicted and analyzed by bioinformatics tools.The results showed that fish β-defensins were hydrophobic cationic antimicrobial peptides.The β-defensin antimicrobial peptide binds to the bacterial membrane through the C-terminal hydrophilic effect,and guides the hydrophobic action of the N-terminal amino acid to insert into the membrane lipid bond to change the permeability of the cell membrane and cause the bacterial biofilm to rupture and die.It was found that β-defensins were heat-resistant and relatively stable,especially ACO88907.1(mandarin fish)and QNV47918.1(striped sea bream)had extremely high heat resistance,which could be applied to many fields other than sterilization.Alpha helices make up the majority of its secondary structure,which has a rather rigid shape.All of its phosphorylation sites,which are dispersed outside of cells,have a signal peptide sequence consisting of 19-20 amino acids that directs the secretion of protein products into an extracellular region.By predicting and analyzing the structure,it can provide ideas for the in-depth study and application of β-defensins and antimicrobial peptide derivatives designs in many fields.
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