Abstract
Newly developed β-1- and β-2-adamantylaspartates [H-Asp(O-1-Ada)-OH and H-Asp(O-2-Ada)-OH] were applied to the sythesis of a C-terminal octapeptide of the β-subunit of human chorionic gonadotropin (hCG) by a conventional solution method and a hexacosapeptide of the α-subunit of insulin receptor (30-55) by a solid-phase method with the objective of suppressing aspartimide formation during the synthesis of aspartylpeptides. The 1-Ada and 2-Ada groups were confirmed to be useful protecting groups for the β-carboxyl function of the Asp residue.