The present study aims to design an artificial metalloprotease based on Zr-containing polyoxometalate, Na8[Zr(W5O18)2] (Zr(W5)2), for the hydrolysis of ovalbumin (OVA) in the presence of different surfactants, which can be used in many areas of biological and medical sciences, particularly for targeted proteolytic drug design. For this reason, parameters including free energy of binding, the chemical nature of amino acid residues, secondary structures, and electrostatic potentials of Zr(W5)2-OVA and Zr(W5)2- OVA-surfactant were analyzed by molecular docking simulations. Investigations showed that the presence of surfactants decreases the binding affinity of Zr(W5)2 to OVA amino acids, and hydrogen bonds and Van der Waals interactions are formed between Zr(W5)2 and OVA amino acids. Additionally, the GROMACS program further illustrated the significance of SDS and CTAB surfactants in influencing the conformational changes of OVA that lead to selective protein hydrolysis. In agreement with molecular dynamics simulation results, the experimental analysis showed higher protein hydrolysis for the Zr(W5)2- OVA-surfactant systems. For instance, circular dichroism spectroscopy indicated that Zr(W5)2-OVACTAB and Zr(W5)2-OVA-TX-100 had higher hydrolytic efficiency due to the increased β-structures rather than α-chains, which showed surfactants can facilitate the accessibility of Zr(W5)2 to the cleavage sites by inducing partial unfolding of the OVA structure

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