As with many different FF, MARTINI v2.1 and v2.2 have limitations. Simulations of proteins and polysaccharides found that the FF had a higher bias for aggregation because of the solute-solute LJ ϵ ij value. These small, but systematic deviations resulted in relatively stronger interactions. Therefore, by reparameterizing the solute-solute interactions, the aggregation behavior is more closely aligned to what is found in experiments and in biology. As of the writing of this dissertation, the most current version of MARTINI is v3, which aims to tackle the aggregation bias of v2.1 and v2.2. MARTINI v3 rebalanced all of the non-bonded interactions and developed newer labels for new bead types. To prove that the rebalancing captured ideal mixing behavior, the radial distribution functions were integrated, known as the Kirkwood-Buff integrals (G ij ). To have ideal mixing behavior, G ij =0, and MARTINI v3 had G ij ≈ 0.3 cm 3 mol , which is fairly low and does not overcompensate the aggregation effects, unlike MARTINI v2.2.