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Conformational behavior of cyclic CCK‐related peptides determined by 400‐MHz 1 H‐nmr: Relationships with affinity and selectivity for brain receptors
Author(s) -
Roy P.,
Charpentier B.,
Durieux C.,
Dor A.,
Roques B. P.
Publication year - 1989
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360280110
Subject(s) - chemistry , moiety , stereochemistry , receptor , selectivity , cyclic peptide , peptide , tyrosine , biochemistry , catalysis
The conformational study of a homogenous series of cyclic analogues of CCK 8 , selective for central receptors, such as Boc‐ X‐Tyr(SO 3 H)‐Nle‐ D ‐Lys ‐Trp‐Nle‐Asp‐Phe‐NH 2 , where X = L ‐Glu, D ‐Glu, or γ‐ D ‐Glu, was performed by 400‐MHz 1 H‐nmr. The regular increase in affinity for central receptors when going from [ L ‐Glu] to [γ‐ D ‐Glu] is correlated to (a) an enhancement in internal flexibility of the cyclic moiety, (b) an external orientation of the tyrosine 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 8 for both receptors types to be performed.