冰鱼抗菌肽Chionodracine的生物信息学分析及其优化肽预测  

Bioinformatics analysis of the icefish antimicrobial peptide Chionodracine and its optimized peptide prediction

作　　者：邓若竹 王娟[1] 牛秋红[1] 胡凡 柯涛[1] DENG Ruozhu;WANG Juan;NIU Qiuhong;HU Fan;KE Tao(Henan Provicial Center for University Biomass Resource Utilization Engineering,College of Life Science,Nanyang Normal University,Nanyang 473061,China;Engineering Technology Research Center for Comprehensive Utilization of Marine Biological Resources,Third Institute of Oceanography,Ministry of Natural Resources,Xiamen 361005,China)

机构地区：[1]南阳师范学院生命科学学院河南省生物质资源化高校工程中心,河南南阳473061 [2]自然资源部第三海洋研究所海洋生物资源综合利用工程技术研究中心,福建厦门361005

出　　处：《黑龙江畜牧兽医》2024年第23期109-115,128,129,共9页Heilongjiang Animal Science And veterinary Medicine

基　　金：国家自然科学基金项目(G180101);河南省科技攻关项目(202102310022)。

摘　　要：为了研究从冰鱼中分离出的抗菌肽Chionodracine及其4种优化肽的生物学功能,试验利用生物信息学软件对其理化性质、二级结构、三级结构、两亲性和修饰位点等进行预测分析,并以冰鱼抗菌肽Chionodracine(母肽)的氨基酸序列为基础,用赖氨酸(K)替换不同位置组氨酸(H)和丝氨酸(S)对该抗菌肽进行优化改造,改造后的抗菌肽命名为Cnd-1~4,并应用生物信息学软件进行预测分析。结果表明:冰鱼抗菌肽Chionodracine是由22个氨基酸组成的阳离子型抗菌肽,其二级结构主要由α-螺旋结构(90.91%)和少量无规则卷曲结构(9.09%)组成,理论等电点为9.99,净电荷为+5,有较高的稳定性和疏水特性,无跨膜区和信号肽,属于细胞膜外蛋白,含有3个磷酸化修饰位点和1个泛素化作用位点,能够被11种蛋白酶剪切,为无毒性蛋白质。在4种优化肽中Cnd-1、Cnd-2、Cnd-3的分子量均小于母肽,理论等电点和正电荷数均比母肽高;二级结构与母肽相似,其中优化肽Cnd-4二级结构中α-螺旋结构占比为95.45%,大于母肽。说明可通过氨基酸位点替换的方式对冰鱼抗菌肽Chionodracine进行优化改造,改造后的冰鱼抗菌肽Chionodracine与细胞膜之间的相互作用及稳定性可能优于母肽。In order to study the antimicrobial peptide Chionodracine isolated from icefish and the biological functions of four optimized peptides,in the experiment,bioinformatics sofware was used to predict and analyze its physical and chemical properties,secondary structure,tertiary structure,amphipathy and modification sites.Based on the amino acid sequence of the icefish antimicrobial peptide Chionodracine(parent peptide),the antimicrobial peptide was optimized by replacing histidine(H)and serine(S)at dfferent positions with lysine(K),and the modified antimicrobial peptide was named Cndl-4,and bioinformatics software were used for predictive analysis.The results showed that Chionodracine was a cationic antimicrobial peptide composed of 22 amino acids.Its secondary structure was mainly composed of aα-helix structure(90.91%)and a small amount of random coils(9.09%),with an isoelectric point of 9.99 and a net charge of+5.It exhibited high stability and hydrophobic characteristics with no transmembrane region and signal peptide,and was an extramembrane protein.It contained 3 phosphorylation modification sites and 1 ubiquitination site,which could be cleaved by 1l kinds of proteases and was a non-toxic protein.Among the four optimized peptides,the relative molecular weights of Cnd-1,Cnd-2 and Cnd-3 were smaller than that of the parent peptide;the theoretical isoelectric point and positive charge number were higher than those of the parent peptide,and the secondary structure was similar to that of the parent peptide.Among them,the proportion ofα-helix structure in the secondary structure of the optimized peptide Cnd-4 was 95.45%,which was larger than that of the parent peptide.The results indicated that the antimicrobial peptide Chionodracine in icefish could be optimized by amino acid site substitution,and the interaction and stability between the icefish antimicrobial peptide Chionodracine and the cell membrane might be better than that of the parent peptide.

关 键 词：冰鱼抗菌肽Chionodracine 生物信息学 稳定性 优化改造 氨基酸序列 

分 类 号：S859.1[农业科学—临床兽医学]