Abstract
A tetracosapeptide (α1-24-ACTH) corresponding to the first 24-amino acid sequence of corticotropin (ACTH) was synthesized by a classical method. The ester exchange method using pentachlorophenyl trichloroacetate (TCAOPCP) was employed successfully for condensation of the main fragments having C-terminal glycine and proline. All protecting groups of the tetracosapeptide were removed using the hydrogen fluoride method. The synthetic peptide thus obtained exhibited an activity of ca. 90 units/mg in in vivo steroidogenic assay.
