Use of N,O‐bis‐Fmoc‐d‐Tyr‐ONSu for introduction of an oxidative iodination site into cholecystokinin family peptides

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Abstract
We report the synthesis of a new reagent for the introduction of an oxidative iodination site into the amino terminus of acid-labile peptides, and the use of this reagent to synthesize a novel affinity-labeling probe for the cholecystokinin (CCK) receptor. The acylation reagent, N,O-bis-fluorenylmethyloxycarbonyl-d-tyrosine hydroxysuccinimide ester, utilizes base-labile protection of both the alpha amino group and the aromatic ring hydroxyl. This can be safely removed to expose a cross-linkable free amino group on the aminopeptidase-resistant d-enantiomer of tyrosine. The synthetic probe, d-Tyr-Gly-Asp-Tyr(OSO3H)-Nle-Gly-Trp-Nle-Asp-Phe-NH2, was fully biologically active, could be radioiodinated to high-specific radioactivity (2000 Ci/mmol), bound with high affinity to the pancreatic CCK receptor, and covalently labeled the hormone-binding site. This reagent should be useful for the synthesis of a wide variety of analogues of CCK and other acid-labile peptides.

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