大肠杆菌中透膜小肽抑制α-Synuclein聚集的研究
Study of Aggregation Inhibition of α-Synuclein with Membrane Permeational Peptides in E.coli
查看参考文献10篇
文摘
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目的:在大肠杆菌中研究透膜小肽抑制α-Synuclein(Α53T,S129Α,WT)的异常聚集.方法:基于α-Syn核心区的疏水区域设计了5种包含7个精氨酸的多聚精氨酸多肽膜透过传输系统的小肽R7P1~R7P5;构建融合蛋白α-Syn-GFP,其中α-Syn基因融合于GFP上游,透膜小肽以双顺反子方式与α-Syn-GFP共表达;以文献报道的可抑制α-Syn异常聚集的小肽ASI1D(MRRGGAVVTG(R)6)为对照,通过监测整体细胞荧光强度研究透膜小肽影响α-Syn(Α53T,S129Α,WT)的异常聚集的情况.结果:5种小肽能不同程度的抑制α-Syn(Α53T,S129Α,WT)的异常聚集;和对照Pc相比,R7P4抑制α-Syn(A53T)异常聚集的效果提高了55%,R7P3抑制α-Syn(S129A)异常聚集的效果提高了64%,R7P4抑制α-Syn(WT)异常聚集的效果提高了39%.结论:在大肠杆菌中,透膜小肽可以有效地抑制α-Syn(Α53T,S129Α,WT)的异常聚集 |
其他语种文摘
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Objective: Study aggregation inhibition of α-Synuclein(Α53T,S129Α,WT) with membrane permeational peptides in E.coli. Method:α-Syn were fussed upstream to GFP to create of a fusion constructs of α-SynG, five membrane permeational peptides R7P1~R7P5 which comes from the hydrophobic region of α-Syn was co-expressed with α-Syn-GFP as a bicistronic. Using the small peptide ASI1D(MRRGGAVVTG(R)6) as control, the ability of the five membrane permeational peptides to aggregation inhibition of α-Syn(A53T,S129A,WT) in E.coli was studied by monitor the whole-cell fluorescence intensity. Result: Five membrane permeational peptides can inhibition the aggregation of α-Syn (A53T,S129A,WT). Compared with ASI1D, for α-Syn (A53T) R7P4 can increase the inhibitory effect by 55%, and for α-Syn (A53T) R7P4 can increase the inhibitory effect by 64%, for α-Syn (A53T) R7P3 can increase the inhibitory effect by 39%. Conclusion: The membrane permeational peptides can inhibition the aggregation of α-Syn (Α53T,S129A,WT) in E.coli |
来源
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生物技术
,2010,20(5):26-29 【扩展库】
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关键词
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α-Synuclein
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透膜小肽
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聚集抑制
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帕金森症
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地址
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1.
湖北工业大学, 湖北省工业微生物重点实验室, 湖北, 武汉, 430068
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湖北生物职业技术学院, 湖北, 武汉, 430068
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湖北工业大学, 湖北省工业微生物重点实验室;;生化工程国家重点实验室, 湖北, 武汉, 430068
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语种
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中文 |
ISSN
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1004-311X |
学科
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分子生物学 |
基金
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国家自然科学基金
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文献收藏号
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CSCD:4068909
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