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A Fluorescence Study on the Interactions of Cationic Lipids with Bovine Serum Albumin
Wu Qihua,Zhu Manzhou,Guo Qingxiang*
Author NameAffiliationE-mail
Wu Qihua Department of ChemistryUniversity of Science and Technology of ChinaHefei 230026  
Zhu Manzhou Structure Research LaboratoryUniversity of Science and Technology of ChinaHefei 230026  
Guo Qingxiang* Department of ChemistryUniversity of Science and Technology of ChinaHefei 230026 qxguo@ustc.edu.cn 
Abstract:
Interactions of a series of dialkyl cationic lipids linking with bovine serum albumin (BSA) through acetal (linker) have been studied by the fluorescence spectroscopy. At low concentrations of cationic lipids, the fluorescence intensity of BSA decreased with binding of cationic lipid, and the maximum of emission wavelength shifted from (344±1)nm to (331±1)nm. It indicates that the BSA goes to uncoiled flexible conformation from its native structure. When the concentrations of lipids increased, the fluorescence intensity increased rapidly and then maintained unchanged. It reveals that two tryptophan residues of BSA are all enwrapped in the bilayer membrane, owing to the hydrophobic interactions between lipids and BSA.
Key words:  Cationic lipid, Acetal, Bovine serum albumin, Fluorescence spectroscopy
FundProject:
含缩醛正离子类脂分子与蛋白质的相互作用
吴其华,朱满洲,郭庆祥*
摘要:
合成系列含缩醛的双链正离子类脂分子,并用荧光光谱研究其与牛血清蛋白(BSA)的相互作用.通过荧光的变化,解释蛋白质构象的变化.在低类脂浓度时,少量类脂分子束缚在牛血清蛋白周围,荧光有很大幅度的淬灭,蛋白质本身肽链被解开,与此同时最大发射波长从(344±1) nm 蓝移到(331±1) nm.由于疏水相互作用,更多类脂分子不断地聚集在蛋白质周围,牛血清蛋白中的两个色氨酸残基被完全地包裹在类脂分子形成的双分子膜中,荧光强度不断增加直到恒定不变.
关键词:  正离子类脂  缩醛  牛血清蛋白  荧光光谱
DOI:10.1088/1674-0068/17/4/476-480
分类号: