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

Abstract

AbstractA tri‐quaternary ammonium salt cationic surfactant was synthesized. Its structure was confirmed by using Fourier‐transform infrared spectroscopy, 1H nuclear magnetic resonance spectroscopy, and X‐ray photoelectron spectroscopy analyses. Three model surfaces, including Au‐CH3, Au‐OH and Au‐COOH, were fabricated. Adsorptions 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‐CH3 surface, and that on the Au‐OH surface. These results suggested that the main driving force of surfactant immobilization was electrostatic interaction followed by hydrophobic interaction. Based on the results obtained, we concluded that the protein mass adsorbed on Au‐CH3‐S, Au‐OH‐S, and Au‐COOH‐S surfaces depended on the protein size and orientation. The 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‐CH3‐S. The Au‐COOH‐S surface could inhibit lysozyme adsorption, maintain the adsorption balance of bovine serum albumin, and induce fibrinogen‐binding protein adsorption.