Additionally, based on our simulations we made a specific prediction for the structure of the aqueous TMA-phenol complex, to be tested by future neutron scattering experiments. Phenol is a particularly relevant aromatic molecule for biological contexts as it mirrors the side chain of tyrosine. Our simulations show that prosECCo75 alters compared to CHARMM36 the overall behavior of these cation-π interactions in a manner similar to TMA-pyridine with the effect effect about twice as strong with phenol as it is for pyridine. Specifically, while CHARMM36 exhibits artefactual phenol aggregation, prosECCo75 predicts a stronger cation-π interaction and yields reduced phenol aggregation. This is also consistent with the known ability of quaternary ammonium ions to enhance solubility of aromatic species. The consistency of the prosECCo75 prediction for both TMA-pyridine and TMA-phenol interactions suggests that the present chargescaling approach may be widely applicable to a broader class of cation-π motifs commonly found in biomolecules, offering a promising strategy for improving the accuracy of molecular dynamics simulations for these complex systems.