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We determine potentials of the mean force for interactions of amino acidswith four common surfaces of ZnO in aqueous solutions. The method involvesall-atom molecular dynamics simulations combined with the umbrella samplingtechnique. The profiled nature of the density of water with the stronglyadsorbed first layer affects the approach of amino acids to the surface andgenerates either repulsion or weak binding. The largest binding energy is foundfor tyrosine interacting with the surface in which the Zn ions are at the top.It is equal to 7 kJ/mol which is comparable to that of the hydrogen bonds in aprotein. This makes the adsorption of amino acids onto the ZnO surface muchweaker than onto the well studied surface of gold. Under vacuum, bindingenergies are more than 40 times stronger (for one of the surfaces). The precisemanner in which water molecules interact with a given surface influences thebinding energies in a way that depends on the surface. Among the fourconsidered surfaces the one with Zn at the top is recognized as binding almostall amino acids with an average binding energy of 2.60 kJ/mol. Another (O atthe top) is non-binding for most amino acids. For binding situations theaverage energy is 0.66 kJ/mol. The remaining two surfaces bind nearly as manyamino acids as they do not and the average binding energies are 1.46 and 1.22kJ/mol. For all of the surfaces the binding energies vary between amino acidssignificantly: the dispersion in the range of 68-154% of the mean. A smallprotein is shown to adsorb onto ZnO only intermittently and with only a smalldeformation. Various adsorption events lead to different patterns in mobilitiesof amino acids within the protein.

Amino acids and proteins at ZnO-water interfaces in molecular dynamics simulations