文献类型：期刊文献

英文题名：Lacticaseibacillus paracasei fermentation broth identified peptide, Y2Fr, and its antibacterial activity on Vibrio parahaemolyticus

作者：Yang, Shen[1,3];Xing, Yufan[1];Gao, Jialong[2];Jin, Ritian[1];Lin, Rong[1];Weng, Wuyin[1];Xie, Yuanhong[1];Aweya, Jude Juventus[1,3]

机构：[1]Jimei Univ, Coll Ocean Food & Biol Engn, Fujian Prov Key Lab Food Microbiol & Enzyme Engn, Xiamen 361021, Fujian, Peoples R China;[2]Guangdong Ocean Univ, Coll Food Sci & Technol, Guangdong Prov Key Lab Aquat Prod Proc & Safety, Zhanjiang 524088, Guangdong, Peoples R China;[3]Jimei Univ, Coll Ocean Food & Biol Engn, Xiamen 361021, Fujian, Peoples R China

年份：2023

卷号：182

外文期刊名：MICROBIAL PATHOGENESIS

收录：SCI-EXPANDED(收录号：WOS:001048910100001)、、Scopus(收录号：2-s2.0-85165611977)、WOS

基金：This work was sponsored by Natural Science Foundation of Xiamen, China (3502Z20227202) , Fund of Guangdong Provincial Key Labora- tory of Aquatic Product Processing and Safety, China (GDPKLAPPS2015) .

语种：英文

外文关键词：Vibrio parahaemolyticus; Lacticaseibacillus paracasei; Antimicrobial peptide; Antibacterial activity; Antibacterial mechanism

外文摘要：Although Vibrio parahaemolyticus infections cause severe diseases of large yellow croaker (Larimichthys crocea), using antibiotics and other chemical agents to treat these infections could result in antimicrobial resistance, environmental pollution, and other associated problems. This study identified seven peptides from Lacticaseibacillus paracasei fermentation broth using ultra-high-performance liquid chromatography-mass spectrometry and screened antimicrobial peptide Y2Fr (VEIKNGLLKLNGKPLLIR) through its net charge, hydrophobicity and predicted secondary structure. Antibacterial activity analysis revealed that Y2Fr had a minimum inhibitory concentration (MIC) of 125 & mu;g/mL, minimum bactericidal concentration (MBC) of 250 & mu;g/mL against V. parahaemolyticus and a time-kill of 3 h. In a bacterial membrane environment, the secondary structure of peptide Y2Fr changed from a random coil to a & beta;-sheet to enhance its membrane permeability and binding to bacteria DNA to exert its antibacterial effect. Further molecular docking analysis revealed that peptide Y2Fr could bind to the membrane protein KKI11460.1 and DNA polymerase A0A0L8TVA4 of V. parahaemolyticus through hydrogen bonds. Meanwhile, treatment of Y2Fr with mammalian red blood cells and plasma revealed that it was noncytotoxic, nonhemolytic, and stable under physiological conditions. Thus, peptide Y2Fr has great potential use in treating and preventing infections caused by V. parahaemolyticus or similar bacteria in aquatic animals.