Experimental study of the ability of oligopeptide trpasp-phe-asp to bind interleukin-8

Background. One of the perspectives of anticytokine therapy is the development of synthetic oligopeptides, which can bind and inhibit the activity of cytokines. The peptide, which is a structural analogue of the cytokine-binding region of the chemokine receptor, is of interest as a ligand for interaction with interleukin-8 (IL-8). The aim of the research was to evaluate the interaction of the Trp-Asp-Phe-Asp with IL-8. Material and methods. The interaction between the peptide and cytokine was evaluated by the change in the IL-8 concentration, which was assessed by enzyme immunoassay. Oligopeptide was used in free form adsorbed on the bottom of the plate well and immobilized in a polyacrylamide gel at a concentration of 1 µM/ml. Results. The results of the study showed that Trp-Asp-Phe-Asp, both in free and immobilized form, has the ability to bind IL-8. The maximum concentration of IL-8 bound by the free peptide is 22.13 (14.09; 30.17) pM/ml, for the adsorbed peptide – 4.22 (3.69; 4.75) pM/ml. Oligopeptide immobilized in the gel reduces the IL-8 concentration in blood plasma by 25.39 (21.34; 29.44) pM/ml. Conclusions. The results obtained are the basis for the development of medical devices for hemosorption in order to extract IL-8 from human blood plasma.