Synthesis of Corticotropin Peptides. XI Synthesis and Biological Properties of [1-β-Alanine]-ACTH(1-18)-Octadecapeptide Amide

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The synthesis is described of an octadecapeptide amide, β-alanyl-tyrosyl-seryl-methionyl-glutamylhistidyl-phenylalanyl-arginyl-tryptophyl-glycyl-lysyl-prolyl-valyl-glycyl-lysyl-lysyl-arginyl-arginine amide, corresponding to the first eighteen amino acid residues of corticotropin except for the amino end which has been substituted by a β-alanine for the serine in native hormone. The adrenalstimulating activities of the octadecapeptide amide are compared with those of the corresponding 1-serine or 1-glycine octadecapeptide amide to show that the 1-β-alanine peptide is remarkably more active than the latter when assayed by in vitro, subcutaneous and intamuscular approaches, and that the activities of the former are maintained for a longer period of time than those of the latter. The 1-β-alanine peptide as a lipotropic agent is also shown to be more active than the synthetic analogs and a native corticotropin on rat adipose tissue. The differences among these octadecapeptide analogs in the biological properties are discussed in terms of their susceptibility toward the action of aminopeptidase.
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