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The hydroxyl-terminated self-assembled monolayer (OH-SAM), as a surfaceresistant to protein adsorption, exhibits substantial potential in applicationssuch as ship navigation and medical implants, and the appropriate strategiesfor designing anti-fouling surfaces are crucial. Here, we employ moleculardynamics simulations and alchemical free energy calculations to systematicallyanalyze the factors influencing resistance to protein adsorption on the SAMsterminated with single or double OH groups at three packing densities ({\Sigma}= 2.0 nm-2, 4.5 nm-2, and 6.5 nm-2), respectively. For the first time, weobserve that the compactness and order of interfacial water enhance itsphysical barrier effect, subsequently enhancing the resistance of SAM toprotein adsorption. Notably, the weak spatial hindrance effect of SAM leads tothe embedding of protein into SAM, resulting in a lack of resistance of SAMtowards protein. Furthermore, the number of hydroxyl groups per unit area ofdouble OH-terminated SAM at {\Sigma} = 6.5 nm-2 is approximately 2 to 3 timesthat of single OH-terminated SAM at {\Sigma} = 6.5 nm-2 and 4.5 nm-2,consequently yielding a weaker resistance of double OH-terminated SAM towardsprotein. Meanwhile, due to the structure of SAM itself, i.e., the formation ofa nearly perfect ice-like hydrogen bond structure, the SAM exhibits the weakestresistance towards protein. This study will complement and improve themechanism of OH-SAM resistance to protein adsorption, especially thetraditional barrier effect of interfacial water.

Factors resisting protein adsorption on hydrophilic/hydrophobic self-assembled monolayers terminated with hydrophilic hydroxyl groups