CFTR第六跨膜区相关肽的二级结构和定位研究  

Study on structure and position of TM6 related peptide of CFTR

作　　者：齐海燕[1] 王颖[1] 马琳[1] 翟明翚[1] QI Hai-yan;WANG Ying;MA Lin;ZHAI Ming-hui(School of Chemistry and Chemical Engineering,Qiqihar University,Qiqihar 161006,China)

机构地区：[1]齐齐哈尔大学化学与化学工程学院

出　　处：《高师理科学刊》2019年第9期56-59,共4页Journal of Science of Teachers＇College and University

基　　金：黑龙江省自然科学基金项目(B2015016);黑龙江省教育厅基本业务专项齐齐哈尔大学科研项目(135109202);黑龙江省教育厅基本业务专项(粮头食尾)(LTSW201732);齐齐哈尔市科技计划项目(SFGG-201607)

摘　　要：采用圆二色光谱和荧光光谱等方法对不同pH值条件下囊性纤维化跨膜传导调节因子(CFTR)的第六跨膜区(TM6)及突变体TM6-R347P在DMPC,DMPG,SDS中的二级结构和定位进行了研究.结果表明,跨膜肽段均插入模型膜的内部并且形成α-螺旋结构;与野生肽段相比突变体α-螺旋含量较少,并且在膜中的位置相对较深,pH值依赖性减小,说明R347P突变影响α-螺旋的形成及在膜中的定位.The secondary structures and positioning of the peptides associated with CFTR-TM6 and TM6-R347P in DMPC,DMPG and SDS at different pH values were investigated by circular dichroism,fluorescence.It was found that all peptides form helix structures and insert into menbranes.The mutation was less structured and embedded in the membranes more deeply than wide peptide at all pH values.The R347P substitution in TM6 significantly impairs the pH dependence.It showed that R347P played a important role in the structure and the location of peptide.

关 键 词：CFTR 二级结构 定位 光谱 

分 类 号：O65[理学—分析化学]