Conformational behavior of cyclic CCK-related peptides determined by 400-MHz 1H-nmr: Relationships with affinity and selectivity for brain receptors
✍ Scribed by P. Roy; B. Charpentier; C. Durieux; A. Dor; B. P. Roques
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1989
- Tongue
- English
- Weight
- 580 KB
- Volume
- 28
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
The conformational study of a homogenous series of cyclic analogues of CCK,, selective for central receptors, such as Boc-X-Tyr(S0,H)-Nle-D-Lys-Trp-Nle-A6psp-Phe-NH,, where X = L-G~u, D-Gh, or Y-D-G~u, was performed by 4W-MHz 'H-nmr. The regular increase in affinity for central receptors when going from [L-Clu] to [Y-D-G~u] k correlated to (a) an enhancement in internal flexibility of the cyclic moiety, (b) an external orientation of the tyrasine side chain, and (c) a restructuring of the C-terminal part of the peptide. All these results could permit a modeling of biologically active conformation of CCK, for both receptors types to be performed.