The artificial receptors functionality is feasible only if the target signal stays independent from other protein sorption processes. The current study is focused on determining the possibility to use the chemistry of the iron-porphyrin complex as a tool for turning haemoglobin-imprinted hydrogel into the protein-receiver with albumin suppressing abilities. Comparison is done according to such criteria as the amount of proteins captured by imprinted and non-imprinted hydrogels without an auxiliary co-monomer, free-base porphyrin and iron-porphyrin. These proteins include bovine haemoglobin and bovine serum albumin. As the main parameters of receptor functionality, the four following factors were considered: high target retention, minimal interference adsorption, the best possible selectivity of the MIP and the highest apparent affinity constant. The only composition meeting the criteria was iron-porphyrin, which demonstrated high amounts of haemoglobin retention (81.2 %), low albumin binding rate (18.5 %), high selectivity (4.40) and appropriate apparent dissociation constant (3.40 × 10−7 M). While the second sample had higher values regarding the amount of haemoglobin captured, it still managed to adsorb a lot of albumin (35.7 %) and achieved selectivity value of 2.17. In its turn, non-modified sample failed to create the required window of difference between proteins – 36.5 percentage points. Thus, the research shows the affirmative answer: yes, the iron centre is changing the function of the receiver due to its ability to retain haemoglobin while suppressing albumin adsorption at the same time.