【摘要】 牛乳铁素（Bovine lactoferricin,Lfcin B）是牛乳铁蛋白经胰酶消化后释放出的17位至41位氨基酸残基构成的短肽，具有广谱抗菌、抗病毒、抗肿瘤和抗寄生虫等生物活性。为了深入开发和利用Lfcin B，进一步去除Lfcin B的部分C-末端氨基酸残基，形成了由10个氨基酸残基构成的短肽，称为Lfcin B_1-10。Lfcin B_1-10较好地保留了Lfcin B的生物活性，但有关Lfcin B_1-10的理化性质、结构、跨膜区等是否改变尚不清楚。因此，利用生物信息学方法对Lfcin B_1-10的氨基酸的理化性质、二级结构、跨膜区、信号肽及酶切位点等特征进行预测分析。结果显示，Lfcin B_1-10为阳离子型抗菌肽，理论等电点为11.71，热稳定性较差；分子为亲水性寡肽，二级结构仅有无规则卷曲，无跨膜区和信号肽，可被机体内多种酶降解，具有良好安全性。研究不仅为深入认识其构效关系、抗菌机制提供依据，同时为Lfcin B_1-10的实际应用提供参考。更多还原

【Abstract】 A short peptide was composed of amino acid residues at positions 17 to 41 released from bovine lactoferrin （Lfcin B）digested by pancreatin.The short peptide had broad-spectrum antibacterial,antiviral,antitumor and antiparasitic activities.In order to further develop Lfcin B,a short peptide composed of 10 amino acid residues was obtained from C-terminal amino acid in Lfcin B.The short peptide was named Lfcin B_1-10.Lfcin B_1-10retained the biological activity of Lfcin B well,but it was not clear that whether the physicochemical properties,structure and transmembrane region of Lfcin B_1-10had changed.Bioinformatics methods were used to predict the characteristics of amino acids in Lfcin B_1-10,such as physicochemical properties,secondary structure,transmembrane region,signal peptide and restriction site.The results showed that Lfcin B_1-10was a cationic antibacterial peptide with a theoretical isoelectric point of 11.71 and poor thermal stability.The molecule is a hydrophilic oligopeptide,and its secondary structure had only irregular curl,no transmembrane region and signal peptide.It could be degraded by various enzymes in the body,and it had good safety,which provided a basis for understanding the structure-activity relationship and antibacterial mechanism of Lfcin B_1-10,but also provided a reference for the practical application of Lfcin B_1-10.更多还原