Molecular dynamics (MD) simulations have been employed to establish a fundamental understanding of how multiple interactions work together to create binding selectivity in chromatographic systems. MD simulations were performed with increasingly complex ligands to identify the key contributors to synergistic interactions in multimodal (MM) ligand-protein systems. The results were used to develop a new technique for mapping synergy between electrostatic and hydrophobic regions on a protein surface and for understanding avidity effects on resins to make predictions of protein retention behavior in MM systems. Simulations were also performed to quantify the effect of mobile phase modifiers in modulating the different types of interactions in MM systems. The knowledge base created using these simulations can be used to select appropriate combinations of MM ligands and modifiers to achieve unique selectivities for challenging protein separations.

Use of molecular simulations to understand and predict multimodal ligand-protein interactions

243rd National Meeting (2012)

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