Dipeptide mimetics can substitute for the receptor activation domain resulting in highly potent analogues of hPTH(1–36)

Abstract A series of hPTH(1–36) analogues were prepared to study the role of the first peptide bond between residues Ser 1 -Val 2 . Some of these analogues were found to show high affinity binding in intact opossum kidney (OK-1) cells and were very active in their ability to stimulate adenylate cyclase production in intact OK-1 cells, rat UMR 106-06 osteosarcoma cells, and SaOS-2 human osteosarcoma cells. A series of hPTH(1–36) analogues were prepared to study the role of the first peptide bond between residues Ser 1 -Val 2 . Some of these analogues were found to be very active in vitro .