ETD

• Gold(I) complexes
• protein fishing
• resin

This project focuses on the immobilization of two gold complexes on solid supports, with the aim of studying the proteomic targets associated with these compounds. For this purpose, 2-CTC resin was employed, onto which suitably modified gold(I) complexes were anchored by optimizing procedures reported in the literature. The gold compounds used were derived from previously studied complexes and were characterized by NMR spectroscopy, elemental analysis, and stability assessments in different solvents (DMSO, PBS, and DMF), in order to evaluate their physicochemical properties prior to immobilization.
From an applicative perspective, the developed system exploits the ability of gold complexes to selectively interact with cysteine or selenocysteine residues exposed on protein side chains. Anchoring to the solid support allows, in the presence of a cell lysate, the isolation of target proteins from the rest of the proteome. To confirm the validity of this strategy, it was first tested with free cysteine, then with human serum albumin (HSA), and finally by performing protein fishing on three model proteins. The results obtained confirm the feasibility of this approach for the study of proteomic targets of gold compounds, paving the way for future applications in proteomics and pharmacology.