The detected probe accretion kinetic effects indicate that the activation energy for exit and entry transitions is sensitive to the composition of the modulating clusters. The asymmetry between the exit rate decelerations (Figure ) and entry rate accelerations (Figure ) implies that variations in cluster composition may influence the energy levels of both the transition state and the micellar ground state (Figure ). In essence, it is possible that both catalysis and thermodynamic changes in affinity levels contribute to the observed kinetics. Validating these energy transformations for different micellar chemistries is a challenging task. Classical MD simulations have been used extensively to determine binding free energies for protein-ligand interactions, using a wide variety of methods for disparate chemical systems . Self-assembling lipid systems, that are dynamic and generate clusters of diverse sizes, compositions and conformations, may prove more tasking to dependably investigate as compared to proteins with more defined binding sites.