大鲵血源抗菌肽AndricinB的生物信息学分析  

Bioinformatics analysis of blood-derived antimicrobial peptide Andricin B of Andrias davidianus

作　　者：任婷 王金泽 郑天骄 王蓓蓓 王梦姣[1] 裴金金 REN Ting;WANG Jinze;ZHENG Tianjiao;WANG Beibei;WANG Mengjiao;PEI Jinjin(College of Biological Sciences and Engineering,Shanxi University of Technology,Hanzhong 723001,China)

机构地区：[1]陕西理工大学生物科学与工程学院,陕西汉中723001

出　　处：《黑龙江畜牧兽医》2021年第22期123-126,153,154,共6页Heilongjiang Animal Science And veterinary Medicine

基　　金：国家自然科学基金青年科学基金项目(3180101528);陕西省高层次人才特殊支持计划项目;陕西省三秦学者创新团队项目。

摘　　要：为研究从大鲵血液中分离鉴定得到的抗菌肽AndricinB的生物学功能,本研究根据已获得的大鲵血源抗菌肽AndricinB氨基酸序列分析其氨基酸组成,采用生物信息学分析工具(软件)分析其理化性质、二级结构、3D构象、信号肽及跨膜区和酶切位点。结果表明:大鲵血源抗菌肽AndricinB含有10个氨基酸残基,分子式为C_(53)H_(92)N_(14)O_(13);分子质量为1133.4 u;理论等电点为11;10个氨基酸残基中,正电荷氨基酸数目为2个,无负电荷氨基酸;在体外哺乳动物网状细胞中半衰期为30 h,在酵母体内的半衰期>20 h,在大肠杆菌体内的半衰期>10 h;不稳定指数为0.51;脂溶性指数为146.0;亲水性平均系数为0.880;二级结构中,无规则卷曲占比为100%;3D构象的能量为-208.339465 kJ/mol,梯度为0.093777;无跨膜区和信号肽;可被多种蛋白酶剪切。说明大鲵血源抗菌肽AndricinB为天然小分子、阳离子型、无规则结构的抗菌肽,虽不利于生物表达与开发应用,但易被体内多种蛋白酶酶解,具有良好的安全性。In order to study the biological functions of the antimicrobial peptide Andricin B isolated and identified from the blood of Andrias davidianus,the amino acid composition of blood-derived antimicrobial peptide Andricin B of Andrias davidianus was analyzed according to its amino acid sequence acquired.The physical and chemical properties,secondary structure,3 D conformation,signal peptide,transmembrane region and enzyme restriction sites were analyzed by bioinformatics analysis tools(software).The results showed that blood-derived antimicrobial peptide Andricin B of Andrias davidianus contained 10 amino acid residues,and the molecular formula was C_(53)H_(92)N_(14)O_(13).Its molecular weight is 1133.4 u.The theoretical isoelectric point is 11.Among the 10 amino acid residues,there were two positively charged amino acids and no negatively charged amino acids.The half-life was 30 h in mammalian reticular cells in vitro,>20 h in yeast,and>10 h in Escherichia coli.Instability index was 0.51.The lipid solubility index was 146.0.The average hydrophilic coefficient was 0.880.In the secondary structure,the proportion of random coil was 100%.The energy of 3 D conformation was-208.339465 kJ/mol,and the gradient was 0.093777.It had no transmembrane region and signal peptide.It could be sheared by a variety of proteases.The results indicated that blood-derived antimicrobial peptide Andricin B of Andrias davidianus was a natural small molecule,cationic and irregular structure antimicrobial peptide.Although it was not conducive to biological expression and development and application,it was easy to be digested by various proteases in vivo and had good safety.

关 键 词：大鲵 抗菌肽 AndricinB 生物信息学分析 二级结构 

分 类 号：S816.73[农业科学—饲料科学] S966.6[农业科学—畜牧学]