Molecular dynamics simulations of amino acid adsorption and transport at the acetonitrile-water-silica interface: the role of side chains.

The solvation and transport of amino acid residues at liquid-solid interfaces have great importance for understanding the mechanism of separation of biomolecules in liquid chromatography. This study uses umbrella sampling molecular dynamics simulations to study the adsorption and transport of three amino acid molecules with different side chains (phenylalanine (Phe), leucine (Leu) and glutamine (Gln)) at the silica-water-acetonitrile interface in liquid chromatography. Free energy analysis shows that the Gln molecule has stronger binding affinity than the other two molecules, indicating the side chain polarity may play a primary role in adsorption at the liquid-solid interface. The Phe molecule with a phenyl side chain exhibits stronger adsorption free energy than Leu with a non-polar side chain, which can be ascribed to the better solvated configuration of Phe. Further analysis of molecular orientations found that the amino acid molecules with apolar side chains (Phe and Leu) have 'standing up' configurations at their stable adsorption state, where the polar functional groups are close to the interface and the side chain is far from the interface, whereas the amino acid molecule with a polar side chain (Gln) chooses the 'lying' configuration, and undergoes a sharp orientation transition when the molecule moves away from the silica surface. Extending our simulation studies to systems with different solute concentrations reveals that there is a decrease in the adsorption free energy as well as surface diffusion as the solute concentration increases, which is related to the crowding in the interfacial layers. This simulation study gives a detailed microscopic description of amino acid molecule solvation and transport at the acetonitrile-water-silica interface in liquid chromatography and will be helpful for understanding the retention mechanism for amino acid separation.