Mechanism of anti-proteins adsorption behavior on superhydrophobic titanium surface

Abstract

Comprehensively understanding the albumin and fibrinogen adsorption behaviors is of fundamental significance for blood-contacting devices to effectively prevent the proteins adsorption. First, a controllable superhydrophobic surface presented great repellence to different liquids with water contact angle 165.2°, plasma contact angle 154.8° and blood contact angle 152.1°. Secondly, the albumin and fibrinogen adhesion tests indicated that the pure titanium surface was fully covered by the proteins layer while only a small amount of the proteins adhered to the superhydrophobic surface. Furthermore, the extended Derjaguin-Landau-Verwey-Overbeek (XDLVO) model was built by considering the Lifshitz-van der Waals (LW), the Lewis acid-base (AB) and the electrostatic double-layer (EL) interactions, the positive value of total interaction energy profile suggested that an overall repulsive interaction between the protein molecules and superhydrophobic surface happened at a small separation distance. Finally, the hollow tubes with inner superhydrophobic surface were implanted into carotid artery of rabbits for two weeks. The content of N element measured by EDS mapping provide a new evidence that superhydrophobic surface owns a great resistance of the proteins absorption, and no thrombosis or blood cells adhered to the superhydrophobic surface. This research revealed the mechanism that superhydrophobic modification could effectively prevent the adsorption of plasma proteins, which could provide some theoretical basis to help design the blood-contacting devices with great hemocompatibility.