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The OH-terminated self-assembled monolayers, as protein-resistant surfaces,have significant potential in biocompatible implant devices, which can avoid orreduce adverse reactions caused by protein adhesion to biomaterial surfaces,such as thrombosis, immune response and inflammation. Here, molecular dynamicssimulations were performed to evaluate the degree of protein adsorption on theself-assembled monolayer terminated with two hydrophilic OH groups ((OH)2-SAM)at the packing densities ({\Sigma}) of 4.5 nm-2 and 6.5 nm-2, respectively. Theresults show that the (OH)2-SAM itself can significantly improve theperformance of its resistance to protein adsorption. This is attributed to thestructure of the (OH)2-SAM itself, i.e., the formation of a nearly perfecthexagonal-ice-like hydrogen bond structure in the OH matrix of the (OH)2-SAM at{\Sigma} = 4.5 nm-2, which sharply reduces the number of hydrogen bonds (i.e.,0.9) formed between the hydrophobic (OH)2-SAM surface and protein. While for{\Sigma} = 6.5 nm-2, the hydrophilic (OH)2-SAM surface can provide morehydrogen bonding sites to form hydrogen bonds (i.e., 7.3) with protein. Thenumber of hydrogen bonds formed between the (OH)2-SAM and protein at {\Sigma} =6.5 nm-2 is ~8 times higher than that at {\Sigma} = 4.5 nm-2, reflecting theexcellent resistance to protein adsorption exhibited by the structure of(OH)2-SAM itself at {\Sigma} = 4.5 nm-2. Compared with traditionally physicalbarrier effect formed by a large number of hydrogen bonds between the (OH)2-SAMand water above at {\Sigma} = 6.5 nm-2, the structure of the (OH)2-SAM itselfat {\Sigma} = 4.5 nm-2 proposed in this study significantly improves resistanceto protein adsorption, which provides new insights into the mechanism ofresistance to protein adsorption on the (OH)2-SAM.

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