Mesoscopic analysis of conformational and entropic contributions to nonspecific adsorption of HP copolymer chains using dynamic Monte Carlo simulations

Dynamic Monte Carlo simulations of short linear HP-type copolymers exhibiting proteinlike characteristics are used to investigate both chain dynamics and changes in chain conformational entropy and their contributions to the energetics of adsorption onto a solid-liquid interface. The dMC results show that the conformations and energies of adsorbed chains are highly degenerate. The ensemble-averaged energy of the adsorbed state is dependent on temperature, chain sequence, native-state stability, and sorbent surface geometry and hydrophobicity. Mesoscopic thermodynamic analyses reveal that, although increased chain conformational entropy contributes to the driving force for adsorption in certain cases, many conditions exist where the change in conformational entropy is either negligible or unfavorable due to constraints imposed by the need to form a large and specific number of favorable intra- and intermolecular contacts and by the impenetrable nature of the sorbent surface. Step-number-averaged energy trajectories, based on sampling of a large number of energy trajectories and thus conformational states at each step number, suggest that the search for a global energy minimum is gradual, so that adsorption is first reversible but becomes apparently irreversible with longer exposure to the sorbent. These results appear to be connected to the conformational adaptability of the chain both on the surface and in solution, and an adsorption model taking chain conformational dynamics into account is proposed.