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- W2085202931 startingPage "1531" @default.
- W2085202931 abstract "Thymopentin (TP5) is a synthetic pentapeptide fragment, which corresponds to position 32 - 36 of thymic polypeptide thymopoietin. Thymopoietin and TP5 display a variety of biological functions, including phenotypic differentiation of T cells and the regulation of immune systems. Previous chemical modification experiments suggested that there was an absolute requirement for N-terminal amino acids to maintain the biological activity of TP5. On the basis of this structure- activity relationship, we designed and synthesized the C-terminally 5-carboxyfluorescein-coupled TP5 (TP5-FAM) as a fluorescent probe for thymopoietin receptor. TP5-FAM could bind to the membrane of human lymphoid cell lines, MOLT-4 cells, in which the thymopoietin receptor is expressed. The binding is specific and saturable (Kd = 33 pM). TP5 and human splenopentin are nearly equipotent inhibitors of TP5-FAM binding to the thymopoietin receptor, but porcine secretin did not show any significant inhibition of TP5-FAM binding to MOLT-4 cells. Thus, TP5-FAM is suggested to be a potent and biologically active ligand that would be useful for studying the binding and functional characteristics of the human thymopoietin receptor." @default.
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- W2085202931 date "2006-12-01" @default.
- W2085202931 modified "2023-09-24" @default.
- W2085202931 title "Chemical Synthesis and Application of C-Terminally 5-Carboxyfluorescein-labelled Thymopentin as a Fluorescent Probe for Thymopoietin Receptor" @default.
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- W2085202931 doi "https://doi.org/10.2116/analsci.22.1531" @default.
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