Eleven-amino acid peptides that mimic the erythropoietin α-helix B increases cell survival in endotheliocyte culture

Aim. To study the cytoprotective activity of peptides that mimic the spatial structure of the erythropoietin α-helix B in vitro. Material and methods. The experiment was performed on the primary cell culture of human endotheliocytes (HUVEC). Hydrogen peroxide (H2O2) was used to mimic oxidative stress. Cells were scattered in 96-well gelatin-coated plates with a density of 5 thousand cells per well. After 24 hours of incubation, the studied peptides were introduced - the basic peptide - Helix B surface peptide HBSP (QEQLERALNSS) and its derivatives EP-11-1 (UEHLERALNSS), EP-11-2 (UEQLERALNCS), EP-11-3 (UEQLERALNTS) in 3 concentrations - 5 μg/ml, 30 μg/ml and 50 μg/ml. Cell viability was measured using the MTT test. Results. Initial screening of the cytoprotective activity of innovative peptides that mimic the erythropoietin α-helix B in vitro was performed.  Our results demonstrate that the original HBSP peptide and its derivatives EP-11-1, EP-11-2, EP-11-3 have a pronounced (p<0.05, compared with the control) cytoprotective effect. Derivatives EP-11-1, EP-11-2 does not differ from the base peptide HBSP in terms of the level of detected activity. When comparing the density of the formazan solution and the percentage of surviving endotheliocytes between the series of experiments with the base peptide HBSP and its derivatives, EP-11-3 showed significant superior cytoprotective effects when compared with HBSP (p<0.05), all over the entire range studied concentrations. Conclusion.  Derivatives of the original peptide with laboratory code EP-11-1, EP-11-2 do not differ in their cytoprotective action from the base peptide HBSP. While the derivatives with laboratory code EP-11-3 presented a higher and significant cytoprotective activity when compared to the base peptide HBS