帮助 关于我们

返回检索结果

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

张亨 1   徐锐 2   王俊卿 1   熊平 1   汪浩勇 3 *  
文摘 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 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 生物技术 ,2010,20(5):26-29 【扩展库】
关键词 α-Synuclein ; 透膜小肽 ; 聚集抑制 ; 帕金森症
地址

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  

2. 湖北生物职业技术学院, 湖北, 武汉, 430068  

3. 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

语种 中文
ISSN 1004-311X
学科 分子生物学
基金 国家自然科学基金
文献收藏号 CSCD:4068909

参考文献 共 10 共1页

1.  Kazantsev A G. Central Role of a - Synuclein Oligomers in Neurodegeneration in Parkinson Disease. Arch Neurol,2008,65(12):1577-1581 被引 4    
2.  Cronin K D. Expansion of the Parkinson disease - associated SNCA - Repl allele upregulates human a - synuclein in transgenic mouse brain. Hum Mol Genet,2009,18(17):3274-3285 被引 3    
3.  Vilar M. The fold of a - synuclein fibrils. Proc Natl Acad Sci USA,2008,105(25):8637-8642 被引 7    
4.  Papapetropoulos S. Clinical phenotype in patients with a - synuclein Parkinson' s disease living in Greece in comparison with patients with sporadic Parkinson' s disease. J Neurol Neurosurg Psychiatry,2001,70(10):662-665 被引 3    
5.  Gorbatyuk O S. The phosphorylation state of Ser - 129 in human a - synuclein determines neurodegeneration in a rat model of Parkinson disease. Proc Natl Acad Sci USA,2008,105(2):764-768 被引 1    
6.  El - Agnaf O. M. A strategy for designing inhibitors of a - synuclein aggregation and toxicity as a novel treatment for Parkinson' s disease and related disorders. FASEB,2004,18(11):1315-1347 被引 1    
7.  Haoyong Wang. Visualization of the Coupled Protein Folding and Binding in Bacteria and Purification of Heterodimeric Complex. Proc Natl Acad Sci USA,2003,100(2):478-483 被引 3    
8.  Du, H. N. A peptide motif consisting of glycine, alanine, and valine is required for the fibrillization and cytotoxicity of human a - synuclein. Biochemistry,2003,42(29):8870-8888 被引 7    
9.  Olanow C W. Is Parkinson' s disease a prion disorder. Proc Natl Acad Sci USA,2009,106(31):12571-12572 被引 2    
10.  El- Agnaf O M A. The N -terminal region of non - A beta component of Alzheimer' s disease amyloid is responsible for its tendency to assume beta - sheet and aggregate to form fibrils. EurJBiochem,1998,258(1):157-163 被引 1    
引证文献 1

1 王俊卿 小肽在原核和真核细胞中抑制α-synuclein异常折叠的研究 生物技术,2011,21(3):29-33
被引 0 次

显示所有1篇文献

论文科学数据集
PlumX Metrics
相关文献

 作者相关
 关键词相关
 参考文献相关

版权所有 ©2008 中国科学院文献情报中心 制作维护:中国科学院文献情报中心
地址:北京中关村北四环西路33号 邮政编码:100190 联系电话:(010)82627496 E-mail:cscd@mail.las.ac.cn 京ICP备05002861号-4 | 京公网安备11010802043238号