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作 者:张炜 杭柏林[1] 董萌萌 胡斌 徐彦召[1] 张慧辉[1] 胡建和[1] Zhang Wei;Hang Bolin;Dong Mengmeng;Hu Bin;Xu Yanzhao;Zhang Huihui;Hu Jianhe(College of Animal Science and Veterinary Medicine,Henan Institute of Science and Technology,Henan Xinxiang 453003)
机构地区:[1]河南科技学院动物科技学院,河南新乡453003
出 处:《现代畜牧兽医》2018年第7期1-9,共9页Modern Journal of Animal Husbandry and Veterinary Medicine
基 金:国家自然科学基金项目(31672559);河南省自然科学基金项目(182300410031);河南省高校科技创新团队支持计划(15IRTSTHN);河南科技学院高层次人才启动项目(2014020)
摘 要:为研究牛源防御素类抗菌肽的生物学功能,本研究利用Prot Param工具分析了抗菌肽的理化性质,利用SOPMA分析了抗菌肽的二级结构,利用NetOGlyc 4.0 Server分析了抗菌肽的糖基化,利用NetPhos 3.1 Server分析了抗菌肽的磷酸化,利用Target P 1.1 Server分析了抗菌肽的亚细胞内定位。结果表明,牛源防御素类抗菌肽为阳离子型抗菌肽,等电点在9.31~11.20之间;TAP、bBD-1、BNBD2、BNBD3、BNBD7、BNBD8和BNBD9为稳定性多肽,其他牛源防御素类抗菌肽为不稳定多肽;BNBD12和BNBD13为疏水性多肽,其他牛源防御素类抗菌肽为亲水性多肽;TAP、LAP、b BD-1、BNBD2、BNBD3、BNBD4、BNBD6、BNBD7、BNBD8和BNBD10由α螺旋、β折叠、β转角和无规则卷曲构成,EBD、BNBD1、BNBD5、BNBD11、BNBD12和BNBD13由β折叠、β转角和无规则卷曲构成;没有糖基化位点,除了BNBD7不存在磷酸化位点外,其他16种防御素类抗菌肽存在丝氨酸和苏氨酸的磷酸化位点,但不存在酪氨酸的磷酸化位点。根据分析结果推测牛源防御素类抗菌肽可作用于细胞壁或细胞膜,从而导致细菌死亡。The test aimed to provide basic information for research the biological function of antimicrobial peptide in bovine defensins(bdAMP).ProtParam tool was utilized to analyze the physicochemical property of bdAMP.SOPMA tool was applied to analyze the secondary structure of bdAMP.NetOGlyc4.0 Server tool and NetPhos3.1Server tool were employed to analyze the glycosylation and phosphorylation of bdAMP respectively.And Target P 1.1Server was used for the analysis of subcellular localization.The results showed that bovine defensins are cationic antimicrobial peptide,and their isoelectric point are between 9.31 and 11.20.TAP,bBD-1,BNBD2,BNBD3,BNBD7,BNBD8 and BNBD9 are stable peptides,other bovine defensins are unstable peptides.BNBD12 and BNBD13 are hydrophobic peptide,and other bovine defensins are hydrophilic peptide.TAP,LAP,bBD-1,BNBD2,BNBD3,BNBD4,BNBD6,BNBD7,BNBD8 and BNBD10 have alpha helix,beta sheet,beta turn and random curl,while EBD,BNBD1,BNBD5,BNBD11,BNBD12 and BNBD13 have beta sheet,beta turn and random curl.Bovine defensins have no glycosylation sites.Except BNBD7 without phosphorylation sites,other 16 kinds of defensins have serine and threonine phosphorylation sites,but there is no tyrosine phosphorylation site.These findings suggested that antimicrobial peptides in bovine defensins could kill bacteria through the interaction with cell wall or cell membrane.
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