The title peptide was originally isolated from the venom of the marine cone snail Conus radiatus in small quantities. The compound has also been obtained by solid-phase peptide synthesis starting from Fmoc-L-proline linked to p-alkoxybenzylalcohol resin (I). Removal of the Fmoc group was effected by treatment with tetrabutylammonium fluoride in DMF. Chain elongation was carried out by coupling with the respective Fmoc-protected amino acids using diisopropyl carbodiimide and 1-hydroxybenzotriazole in CH2Cl2-DMF, followed by deprotection cycles with tetrabutylammonium fluoride. Gamma-carboxy glutamic acid was incorporated as the protected bis-tert-butyl ester. The final protected peptide resin (III) was liberated and deprotected by using a mixture of trifluoroacetic acid, thioanisole, water, ethanedithiol and dichloromethane, and the resulting peptide was air oxidized at a pH of 7.8 to form the required disulfide bridge.

The title peptide was originally isolated from the venom of the marine cone snail Conus radiatus in small quantities. The compound has also been obtained by solid-phase peptide synthesis starting from Fmoc-L-proline linked to p-alkoxybenzylalcohol resin (I). Removal of the Fmoc group was effected by treatment with tetrabutylammonium fluoride in DMF. Chain elongation was carried out by coupling with the respective Fmoc-protected amino acids using diisopropyl carbodiimide and 1-hydroxybenzotriazole in CH2Cl2-DMF, followed by deprotection cycles with tetrabutylammonium fluoride. Gamma-carboxy glutamic acid was incorporated as the protected bis-tert-butyl ester. The final protected peptide resin (III) was liberated and deprotected by using a mixture of trifluoroacetic acid, thioanisole, water, ethanedithiol and dichloromethane, and the resulting peptide was air oxidized at a pH of 7.8 to form the required disulfide bridge.

The title peptide was originally isolated from the venom of the marine cone snail Conus radiatus in small quantities. The compound has also been obtained by solid-phase peptide synthesis starting from Fmoc-L-proline linked to p-alkoxybenzylalcohol resin (I). Removal of the Fmoc group was effected by treatment with tetrabutylammonium fluoride in DMF. Chain elongation was carried out by coupling with the respective Fmoc-protected amino acids using diisopropyl carbodiimide and 1-hydroxybenzotriazole in CH2Cl2-DMF, followed by deprotection cycles with tetrabutylammonium fluoride. Gamma-carboxy glutamic acid was incorporated as the protected bis-tert-butyl ester. The final protected peptide resin (III) was liberated and deprotected by using a mixture of trifluoroacetic acid, thioanisole, water, ethanedithiol and dichloromethane, and the resulting peptide was air oxidized at a pH of 7.8 to form the required disulfide bridge.