Interaction of Plasma Proteins with Tri-quaternary Ammonium Salt Cationic Surfactant Studied by QCM-D

作     者：Man Xi Baoyan Zhang 

作者机构：Research Center for Molecular Science and EngineeringNortheastern UniversityShenyangLiaoning 110819China 

出 版 物：《Chinese Journal of Chemistry》 (中国化学（英文版）)

年 卷 期：2015年第33卷第2期

页      面：253-260页

核心收录：

学科分类：081704[工学-应用化学] 07[理学] 070304[理学-物理化学(含∶化学物理)] 08[工学] 0817[工学-化学工程与技术] 0703[理学-化学] 

基　　金：the National Natural Science Fundamental Committee of China and HI-Tech Research and the Development Program(863 No.2006AA02Z291)of China 

主　　题：tri-quaternary ammonium salt cationic surfactant self-assembled monolayers quartz crystal micro-balance with dissipation(QCM-D) proteins adsorption 

摘      要：A tri-quaternary ammonium salt cationic surfactant was *** structure was confirmed by using Fourier-transform infrared spectroscopy,^(1)H nuclear magnetic resonance spectroscopy,and X-ray photoelectron spectroscopy *** model surfaces,including Au-CH_(3),Au-OH and Au-COOH,were *** of surfactant on the three model surfaces and subsequent plasma proteins adsorption were investigated by quartz crystal microbalance with dissipation(QCM-D).The mass of surfactant on the Au-COOH surface was the largest,followed by that on the Au-CH_(3)surface,and that on the Au-OH *** results suggested that the main driving force of surfactant immobilization was electrostatic interaction followed by hydrophobic *** on the results obtained,we concluded that the protein mass adsorbed on Au-CH_(3)-S,Au-OH-S,and Au-COOH-S surfaces depended on the protein size and *** mass and thickness of S on the Au-COOH surface is the largest and the protein adsorption capacity of Au-COOH-S surface is inferior to that of Au-CH_(3)-*** Au-COOH-S surface could inhibit lysozyme adsorption,maintain the adsorption balance of bovine serum albumin,and induce fibrinogen-binding protein adsorption.