Unexpectedly resisting protein adsorption on self-assembled monolayers terminated with two hydrophilic hydroxyl groups.

Abstract

OH-terminated self-assembled monolayers, as protein-resistant surfaces, have significant potential in biocompatible implant devices, which can avoid or reduce adverse reactions caused by protein adhesion to biomaterial surfaces, such as thrombosis, immune response and inflammation. Here, molecular dynamics simulations were performed to evaluate the degree of protein adsorption on the self-assembled monolayer terminated with two hydrophilic OH groups ((OH)2-SAM) at packing densities (Σ) of 4.5 nm-2 and 6.5 nm-2, respectively. The results show that the structure of the (OH)2-SAM itself, i.e., a nearly perfect hexagonal-ice-like hydrogen bond structure in the OH matrix of the (OH)2-SAM at Σ = 4.5 nm-2 sharply reduces the number of hydrogen bonds (i.e., 0.7 ± 0.27) formed between the hydrophobic (OH)2-SAM surface and protein. While for Σ = 6.5 nm-2, the hydrophilic (OH)2-SAM surface can provide more hydrogen bonding sites to form hydrogen bonds (i.e., 6.2 ± 1.07) with protein. The number of hydrogen bonds formed between the (OH)2-SAM and protein at Σ = 6.5 nm-2 is ∼8 times higher than that at Σ = 4.5 nm-2, reflecting the excellent resistance to protein adsorption exhibited by the structure of the (OH)2-SAM itself at Σ = 4.5 nm-2. Compared with a traditional physical barrier effect formed by a large number of hydrogen bonds between the (OH)2-SAM and water at Σ = 6.5 nm-2, the structure of the (OH)2-SAM itself at Σ = 4.5 nm-2 proposed in this study significantly improves the performance of the (OH)2-SAM resistance to protein adsorption, which provides new insights into the mechanism of resistance to protein adsorption on the (OH)2-SAM.