Abstract
Membrane fouling phenomena, which can be promoted by the adsorption of various foulants such as proteins, have been one of the significant challenges in membrane separation. In this study, to conduct a theoretical design of an antifouling membrane material, free energy calculations are performed from molecular dynamics simulations. Particularly, the intermolecular affinities between an amino acid residue and a repeating unit of a candidate material are assessed, by calculating free energy profiles for a residue approaching a repeating unit in explicit water molecules. The predicted profiles for highly biocompatible materials have almost no energetically stable points, regardless of the type of residue. In contrast, the profiles for conventional materials show some energetically remarkable minima. These results agree with previous experimental reports of differences in the amount of protein adsorbed on these materials. Further applications of free energy calculations certainly lead to the development of drastically simplified screening approaches of an optimal antifouling material.
