Ring Size of Somatostatin Analogues (ODT-8) Modulates Receptor Selectivity and Binding Affinity.

[摘要]：The synthesis, biol. testing, and NMR studies of several analogs of H-cyclo[Cys3-Phe6-Phe7-D-Trp8-Lys9-Thr10-Phe11-Cys14]-OH (ODT-8, a pan-somatostatin analog, 1) have been performed to assess the effect of changing the stereochem. and the no. of atoms in the disulfide bridge on binding affinity. Cysteine at positions 3 and/or 14 (somatostatin numbering) were/was substituted with D-cysteine, norcysteine, D-norcysteine, homocysteine, and/or D-homocysteine. The 3D structure anal. of selected partially selective, bioactive analogs (compds. 3 18, 19 and 21) was carried out in dimethylsulfoxide. Interestingly and not unexpectedly, the 3D structures of these analogs comprised the pharmacophore for which the analogs had the highest binding affinities (i.e., sst4 in all cases).

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