Small peptides such as dipeptides contribute to a great extent to the characteristic taste of dry-cured hams. In this study, hydrophilic interaction liquid chromatography (HILIC) combined to tandem mass spectrometry was used to separate, identify, and quantify seven dipeptides in dry-cured hams sampled at different processing times (6, 12, 18, and 24 months). Results showed an increased concentration of dipeptides DA, DG, EE, ES, and EV with the length of processing, obtaining values up to 23 mu g/g of dry-cured ham, which suggests an intense action of muscle enzymes dipeptidyl peptidases during the process. The dipeptide VG significantly decreased from 7 to 4 mu g/g of dry-cured ham as the processing increased from 6 to 24 months, whereas the dipeptide PA showed low values between 380 and 550 ng/g of dry-cured ham at all the sampling times. Additionally, in silico analyses reported the sensory characteristics of the studied dipeptides, mostly giving bitter and umami taste, and predicted their allergenicity, toxicity, and physicochemical properties. These results could be useful for further studies related to the pleasant taste of dry-cured hams.