Tissue integrity and hence human health are both influenced by cell attachment to the extracellular matrix. Integrins are heterodimer cell surface receptors made up of two non-covalently coupled alpha and beta subunits that primarily govern cell motility, adhesion, differentiation, migration, and proliferation by interacting with cell-cell adhesion and cell-extracellular matrix. Integrin α5β1, also known as the ‘fibronectin receptor’, is a heterodimer composed of α5 and β1 subunits that has emerged as a key mediator in several human carcinomas. Several forms of human malignancies, including cell proliferation, angiogenesis, and tumor spread, are intimately associated with this kind of integrin. The purpose of this work is the search for small inhibitor molecules capable of downregulating the interactions between α5β1 and fibronectin.