Hydrophobic amino acid adsorption on surfaces of varying wettability

The adsorption behavior of the model nonpolar amino acid leucine at a solid surface of tunable wetting ability has been examined by means of molecular dynamics simulation. When leucine adsorbs at a highly hydrophobic surface it is found to orient itself with its nonpolar side chain toward the surface and its charged amine and carboxyl groups directed toward the bulk. When the surface is less hydrophobic, leucine alternates between two stable orientations, a standing orientation like that observed at nonwetting surfaces, and a laying orientation in which its side chain and charged groups are located nearly the same distance from the surface. These results are rationalized by a water-density-dependent ordering scheme in which interfacial water structure governs the adsorbed structures. We pay particular attention to how the structure of surface water is changed in the presence of adsorbed leucine in both orientations. We propose that a water density model may be applied as a general technique for understanding adsorption from solution at solid hydrophobic surfaces.