Synthesis of Corticotropin Peptides. XII. The Effect of Amino-terminal Substitution in the Corticotropin 1-18 Peptide

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The synthesis and biological properties are described of an octadecapeptide amide, α-aminoisobutyryl-tyrosyl-seryl-methionyl-glutamyl-histidyl-phenylalanyl-arginyl-tryptophyl-glycyl-lysylprolyl-valyl-glycyl-lysyl-lysyl-arginyl-arginine amide, corresponding to the first eighteen amino acid residues of corticotropin (ACTH) except for the amino terminal residue. The amino-terminal decapeptide as intermediate is built up from a tripeptide (positions 1–3) and a heptapeptide (4–10), where a benzyloxycarbonyl and a benzyl ester groups are used for protection of the terminal α-amino group and the γ-carboxyl group of 5-glutamic acid, respectively. These protecting groups are removed in the final step with hydrogen fluoride. The new method is successfully applied to the corresponding 1-β-alanine octadecapeptide amide, which has been synthesized previously by a different procedure. Adrenal-stimulating properties of the 1-α-aminoisobutyric acid peptide are compared with those of the 1-β-alanine peptide to show that the former peptide is more active than the latter when assayed by the adrenal-ascorbic acid depletion and the <I>in vivo</I> steroidogenesis methods. The lipotropic activity of the new peptide is also shown to be more prolonged than that of the 1-β-alanine peptide.
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