Reliable solubility data is crucial for controlling and optimising crystallisation conditions, to provide a cost-effective purification method with the potential for scaling up. This study investigated the effect of amino acid sequence on determining peptides solubility behaviours. Four dipeptides with different sequences and combinations of alanine and glycine were selected to study their temperature dependent (283.15 K to 313.15 K) aqueous solubilities and solubility in the presence of ethanol and DMSO as antisolvent at 298.15 K. Aqueous solubility data of dipeptides presents the following order: glycyl-L-alanine (gly-ala) > L-alanyl-L-alanine (ala-ala) > glycyl glycine (gly-gly) > L-alanyl glycine (ala-gly). This solubility order has been substantiated by solvation free energy calculations using molecular dynamics (MD) simulations, providing insights into the underlying molecular interactions that govern these solubility patterns. The solubility data also demonstrated difference in the temperature dependency that: gly-gly > gly-ala > ala-gly > ala-ala, corresponding to their dissolution enthalpy order. In the presence of antisolvent range from 0 % to 80 % (by mass) concentration, peptide’s solubility was more susceptible to DMSO than ethanol. Accurate prediction of the solubilities validated the effectiveness of non-random two-liquid (NRTL) model for peptide studies.