| abstract |
Novel hormonogen forms of biologically active vasopressin and its synthetic analogs having extended half-lives and improved activity are obtained by attaching a side peptide chain containing from 1 to about 3 amino acid residues to the free amino group of an alpha-amino acid residue having a basic side chain. Preferred hormogens may be represented by the structural formula: <CHEM> wherein A is hydrogen, hydroxy or lower alkoxy, especially methoxy, B is the peptide residue of phenylalanine (Phe) or isoleucine (Ile), D is the peptide residue of glutamine (Gln) or valine (Val), Asn represents the peptide residue of asparagine, E represents the peptide residue of proline (Pro), 4-thioproline (4-thioPro) or 3,4-dehydroproline (3,4-dehydroPro)FNHX represents an N-substituted peptide residue of L- or D-lysine (Lys) or L- or D- ornithine (Orn), X represents a side peptide chain as previously defined, G is disulfide (-S-S-) or thioether (CH2S- or -SCH2-) and J is the peptide residue of glycine (Gly), L-Alanine (L-Ala) or D-Alanine (D-Ala). |