Journal of labelled compounds and radiopharmaceuticals p. 817 - 826 (1997)
Update date:2022-08-04
Topics:
Darula, Zsuzsa
Peter, Antal
Toth, Geza
New conformationally constrained deltorphin I and II analogues were designed and synthesized, using a more lipophilic amino acid (Ile) instead of Val at positions 5 and 6, and 2-aminotetralin-2-carboxylic acid (Atc) at position 3. Two analogues (Tyr-D-Ala-(S)-Atc-Asp-Ile-Ile-Gly-NH2 and Tyr-D-Ala-(R)-Atc-Glu-Ile-Ile-Gly-NH2) with high potency and selectivity for δ opioid receptors were chosen for tritiation, with 3,5-I2-Tyr1-deltorphin analogues as precursors. Catalytic dehalotritiation of these precursors resulted in tritiated peptides with high specific radioactivity (1.28 TBq/mmol (34.5 Ci/mmol) and 1.33 TBq/mmol (36.0 Ci/mmol), respectively).
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Doi:10.1016/S0277-5387(96)00390-7
(1997)Doi:10.1039/a606159a
(1997)Doi:10.1021/jm010357t
(2002)Doi:10.1016/S0022-328X(96)06331-0
(1997)Doi:10.1016/S0040-4039(97)00167-6
(1997)Doi:10.1016/S0040-4039(97)00211-6
(1997)