Abstract Background: Dopamine (DA) is an important neurotransmitter with a fundamental role in regulatory functions related to the central, peripheral, renal, and hormonal nervous systems. Dopaminergic neurotransmission dysfunctions are commonly associated with several diseases; thus, in situ quantification of DA is a major challenge. To achieve this goal, enzyme-based biosensors have been employed for substrate recognition in the past. However, owing to their sensitivity to changes in temperature and pH levels. Results: New peptide bioreceptors have been developed. Based on this, 45 in silico bioreceptors were designed to exhibit a higher affinity than that of the DA transporters (DATs). The design was based on the active sites of crystallized enzyme structures that are physiologically related to DA. These affinities were calculated using AutoDock Vina and by assessing the interaction energy between DA and the active DAT site. The controlled variables in the design were amino acids, bond type, steric volume, stereochemistry, affinity, and interaction distances. Conclusions: Three bioreceptor candidates presenting promising values ​​in terms of DA affinity and distance were obtained.