家蝇天蚕素-人溶菌酶融合蛋白的生物信息学分析  

Bioinformatic analysis of Musca domestica cecropin-human lysozyme fusion protein

作　　者：卢雪梅[1] 金小宝[1] 朱家勇[1] 黄演婷[1] 

机构地区：[1]广东药学院药用生物活性物质研究所/广东省生物活性药物研究重点实验室,广东广州510006

出　　处：《广东药学院学报》2012年第2期192-195,共4页Academic Journal of Guangdong College of Pharmacy

基　　金：国家自然科学基金(30671832)

摘　　要：目的利用生物信息学方法分析家蝇天蚕素-人溶菌酶融合基因推导的氨基酸序列。方法用ProtParam Tool、CDD、ProtScal、sopma等软件对其理化性质、疏水性/亲水性、信号肽、功能结构域及蛋白质二级结构等重要参数进行预测。结果家蝇天蚕素-人溶菌酶由187个氨基酸组成,预测相对分子质量为20 131.7,理论等电点(pI)为9.69,分子式为C862H1375N277O260S11;半衰期预测结果显示其利于基因工程表达。融合蛋白的氨基酸序列含有天蚕素家族和溶菌酶家族二者的保守结构域,二级结构主要由α-螺旋、β-折叠、β-转角和无规则卷曲组成。结论分析结果为家蝇天蚕素-人溶菌酶融合基因的原核表达及表达产物的生物学功能研究奠定了基础。Objective To analyze the amino acid sequences of Musca domestica cecropin-human lysozyme（Mdc-HLY） fusion protein by bioinformatics analysis.Methods The physical-chemical properties,hydrophobicity or hydrophilicity,the signal peptide,the conserved domains and protein secondary structure of Mdc-HLY were analyzed by ProtParam Tool,CDD,ProtScal,sopma et al.Results Mdc-HLY was cationic molecules and was composed of 187 amino acids,with molecular weight of 20 131.7,theoretical PI of 9.69,the structural formula of C862H1375N277O260S11.The fusion protein included the conserved domains of both Musca domestica cecropin and human lysozyme.Instability index classified the protein as stable,and conducive to its expression using genetic engineering.The secondary structure of Mdc-HLY contained α-helix,β-sheet,β-turn and random coil.Conclusion These results may provide foundation for further study on the expression and biological activity of Mdc-HLY.

关 键 词：家蝇天蚕素 人溶菌酶 融合蛋白 生物信息学分析 

分 类 号：Q78[生物学—分子生物学]