1976 Volume 49 Issue 12 Pages 3615-3619
The final coupling, deprotection and purification processes for the synthesis of octadecapeptides, H–Ser–Tyr–Ser–Met–Glu–His–Phe–Arg–Trp–Gly–Lys–Pro–Val–Gly–Lys–Lys–Arg–Arg–OH(I) and H–Ser–Tyr–Ser–Met–Glu–His–Phe–Arg–Trp–Gly–Lys–Pro–Val–Gly–Lys–Lys–Arg–Arg–NH2 (II), corresponding to the first eighteen amino acid residues of corticotropin (ACTH) are described, in which the N-hydroxysuccinimide ester of the N-terminal decapeptide derivative is coupled with the C-terminal octapeptide and octapeptide amide derivatives to give the two protected end products. The same decapeptide active ester is also utilized to the synthesis of a nonadecapeptide, H–Ser–Tyr–Ser–Met–Glu–His–Phe–Arg–Trp–Gly–Lys–Pro–Val–Gly–Lys–Lys–Arg–Arg–Pro–NH2 (III), identical with the first nineteen amino acid residues of ACTH. The in vivo steroidogenic potencies of the synthetic peptides are compared with that of the synthetic human ACTH (αh-ACTH) as reference to show that the relative potencies of I, II, and III vs. αh-ACTH are 0.14, 0.48, and 0.47, respectively, as estimated on a molar basis.
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