Frederix et al. addressed this self-assembly problem with computational theoretical chemistry. They systematically screened all 8,000 possible tripeptide sequences for their aggregation propensity in water. Using coarse-grained MD simulations, they developed an aggregation propensity score. They introduced a hydrophilicity-corrected version to prioritize peptides that balance self-assembly with water solubility. Their analysis revealed that aromatic residues such as phenylalanine, tyrosine, and tryptophan promote aggregation when placed in the second or third position, while positively charged or hydrogen-bonding residues at the Nterminus and negatively charged residues at the C-terminus enhance self-assembly.