Study of USH3 self-association phenomenon induced by a drug

Abstract

The gene of the c-Src protein was the first oncogene to be discovered. This protein is a non-receptor tyrosine kinase, present and necessary in the human cell. C-Src features a disordered "unique domain" region that together with the SH3 domain form a diffuse complex, which unlike what was thought until recently, plays a significant role in activating and disabling the protein. This protein, in its activated state, is often overexpressed in oncogenic signalling pathways, playing a significant role in promoting the progression of many types of cancer and tumour growth. Several multi-pharmacological therapies have been developed to target this protein, without producing satisfactory results, either because they have not shown effectiveness or because of their associated toxicity. Recent studies have shown that a drug used to target the disordered region of another hepatitis-associated protein could also be effective in the disordered c-Src region. Although the possible mechanism of action of the drug in c-Src is still being studied, it is thought that it could inhibit the protein by enhancing its aggregation. The aim of this study was to explore this hypothesis, measuring the size of the protein's hydrodynamic radius when interacting with the drug using Dynamic Light Scattering (DLS), a technique which provides information in molecular dynamics