Experimental study of the ability of oligopeptide trpasp-phe-asp to bind interleukin-8
Journal of the Grodno State Medical University(2022)
Abstract
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.
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Key words
trpasp-phe-asp
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