Purification and Activity Evaluation of a Novel Thrombopoietin Mimetic Peptide

The emergence of thrombopoietin mimetic peptides presents a promising therapeutic strategy for addressing thrombocytopenia. This particular study aimed to establish a direct, expeditious, and efficient method for modifying and purifying a novel thrombopoietin mimetic peptide. Precursor proteins were subjected to modification utilizing three distinct fatty acids: C₂₅H₄₂O₇N₂, C₃₉H₆₆O₁₅N₄, and C₄₁H₇₀O₁₅N₄. Liquid chromatography analyses demonstrated that C₄₁H₇₀O₁₅N₄ yielded the most effective modification results. Mass spectrometry findings validated the correspondence between the theoretical and actual molecular weights of each sample. In vivo experiments conducted on normal mice showcased that the C₄₁H₇₀O₁₅N₄ modification group exhibited the highest platelet count, peaking at an impressive 5047 × 10⁹/L. This count was approximately twice that of the peak platelet count observed in the dTMP group and four times higher than the control group. Pharmacokinetic investigations revealed that the C₄₁H₇₀O₁₅N₄ modification group displayed the lengthiest half-life among beagles, persisting for 128.5 h. This duration was approximately 28.5 times longer than that of the unmodified dTMP group. These findings underscore the effectiveness of the established C₄₁H₇₀O₁₅N₄ modification and purification method in preserving the biological activity of the thrombopoietin mimetic peptide. The novel thrombopoietin mimetic peptide showcased notable attributes of simplicity and cost-effectiveness, while also exhibiting a significant platelet-promoting effect and an extended half-life. Consequently, this novel peptide holds substantial significance for advancing the treatment of thrombocytopenia.