A study on druggability of MIA as a promising approach for inhibition of metastasis.

MIA (Melanoma Inhibitory Activity) protein is over expressed in melanoma cells and binds to extracellular matrix proteins as well as to several integrins. These interactions were suggested to promote formation of metastasis. Therefore, abrogation of MIA interaction with other proteins using small molecules might show a diminishing effect on cancer cell invasion. The present study is aimed at the analysis of the integrin-binding site of MIA using molecular docking, followed by a virtual screening for drug-like compounds that show potential as putative inhibitors of MIA-integrin interaction. Results showed that at the proposed binding interface of the MIA-integrin complex, a druggable binding pocket is located. Therefore, the integrin-binding domain of MIA was used as a receptor to screen 2200 drug-like compounds. Next, we analysed the interactions of the identified hit compounds with the MIA binding pocket to find the most important features of the hit compounds.