Abstract
We report a high affinity, mu opioid receptor selective enkephalin analogue in which the N-terminal tyrosine residue thought to be required for such high affinity is replaced by phenylalanine. The high affinity can be traced to a shift of the ligand's N-terminal residue within the mu receptor binding pocket, which diminishes the importance of the usual hydrogen bond between the tyrosine phenolic moiety and the receptor.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Enkephalins / chemical synthesis
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Enkephalins / metabolism*
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Enkephalins / pharmacology*
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Kinetics
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Peptides, Cyclic / chemistry
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Peptides, Cyclic / metabolism
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Peptides, Cyclic / pharmacology
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Receptors, Opioid, mu / drug effects*
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Receptors, Opioid, mu / metabolism*
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Structure-Activity Relationship
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Tyrosine / chemistry*
Substances
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Enkephalins
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Peptides, Cyclic
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Receptors, Opioid, mu
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Tyrosine