Three cyclic disulfide analogs related to somatostatin, D-Phe1-Cys2-Tyr3-D-Trp4-Lys5-Thr6-Xxx7-Thr8NH2 (where Xxx = L-Pen 1; L-Cys 3; or D-Pen 4) were examined in DMSO-d6 by one- and two-dimensional proton n.m.r. spectroscopy in order to analyze the conformational influence of the position-7 residue on the 20-membered disulfide ring. From these studies it was concluded that all three analogs maintain a β II' turn solution conformation for the core tetrapeptide-Tyr3-D-Trp4-Lys5-Thr6-. However, the disulfide conformation differs in the analogs, with 1 and 3 having a left-handed and 4 a right-handed disulfide chirality.
|Original language||English (US)|
|Number of pages||9|
|Journal||International Journal of Peptide and Protein Research|
|Publication status||Published - 1988|
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