## Synopsis The strategy and tactics of conformational analysis of cyclic peptides in solution is demonstrated by the example of cyclo(-D-Pro-Phe-TPhe-TYp-Phe-). Spin-locked experiments like rotating frame nuclear Overhauser enhancement spectroscopy (ROESY), ROTO, and TOCSY are successfully applie
Conformational analysis of two cyclic disulfide peptides
✍ Scribed by C. García-Echeverría; G. Siligardi; P. Mascagni; W. Gibbons; E. Giralt; M. Pons
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1991
- Tongue
- English
- Weight
- 636 KB
- Volume
- 31
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
bonds have been carried out in different solvents to investigate the formation and stabilization of @-turn structures and to determine the stereochemistry of the disulfide linkage.
Both peptides have three-dimensional structures with a type I1 P-turn, as derived from quantitative nuclear Overhauser effect data. The combined use of CD and nmr indicates that the dihedral angle of the disulfide bridge is different in the two peptides, although the chirality is maintained.
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A 20-membered cyclic peptide disulfide Boc-C ys-Val-Aib-Ma-Leu-C ys-NHMe I I S S has been synthesized as a conformational model for disulfide loops of limited ring size. 'H-nmr studies at 270 MHz establish the presence of three intramolecular hydrogen bonds involving the Leu, Val, and methylamide NH
The allowed conformations of the p-receptor-selective cyclic opioid peptide analog H-Tyr-D-Om-Phe-Asp-NH, were determined using a grid search through the entire conformational space. Energy mnimization of the 13-membered ring structure lacking the exocyclic Tyr' residue and the Phe3 side chain using