ArticleBiotechnology letters2023
Improving pharmacological activities of thrombopoietin mimetic peptide by genetic fusion to albumin-binding domain.
Article in Biotechnology letters, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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1 citing paper in PubMed, 3 citations in OpenAlex.
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4 authors at 3 institutions in 1 country.
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Abstract
objectiveThrombopoietin mimetic peptide (TMP), an analog of natural thrombopoietin, can be used to treat primary immune thrombocytopenia. However, the short half-life of TMP limits its application in clinics. The present study aimed to improve the stability and biological activity of TMP in vivo via genetic fusion to the albumin-binding protein domain (ABD).
resultsTMP dimer was genetically fused to the N-terminal or C-terminal of ABD, denoted as TMP-TMP-ABD and ABD-TMP-TMP. A Trx-tag was used to improve the fusion proteins' expression levels effectively. ABD-fusion TMP proteins were produced in Escherichia coli and purified by Ni
conclusionsABD can effectively improve the stability and pharmacological activity of TMP by binding to serum albumin, and the ABD-fusion TMP protein can promote platelet formation in vivo.
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