Historically, an important strategy for disrupting the adhesion of integrins to their ligands is by using a synthetic peptide th
at mimics the binding site on the ECM molecule to which the integrin attaches. In the case of fibronectin, the amino acid sequence is arginine-glycine-aspartate (when written using the single letter designation for each amino acid, this sequence becomes RGD). Explain why addition of such synthetic peptides would disrupt binding of cells to their normal substratum.
Upon binding of integrins with such synthetic peptides, disrupts the receptors, and make them unavailable to bind with fibronectin or laminin.
It would impact in inhibition of binding of cells to extracellular matrix (ECM). It is an important strategy that disrupts the adhesion of integrins and ligands. It can have significant role in tumor invasion and metastasis.
