Abstract
[reaction: see text] Ohmefentanyl binds to the rat mu-opiod receptor via two dipeptide sequences (Trp-His and Asp-Tyr) that are separated by 170 residues. A turn-inducing tripeptide, Pro-Aib-Aib, holds the dipeptides in a conformation that binds the narcotic (K(b) = 7.1 x 10(4) M(-)(1)) in THF. Binding is specific for ohmefentanyl over morphine and is accompanied by a conformational change in the heptapeptide host. Control experiments with a Gly-Gly-Gly tripeptide linking the dipeptides show no evidence of binding.
Publication types
-
Research Support, N.I.H., Extramural
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, Non-P.H.S.
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Dipeptides / chemistry
-
Fentanyl / analogs & derivatives*
-
Fentanyl / chemistry*
-
Fentanyl / pharmacology
-
Molecular Mimicry
-
Molecular Structure
-
Morphine / pharmacology
-
Peptides / chemistry*
-
Rats
-
Receptors, Opioid, mu / chemistry*
Substances
-
Dipeptides
-
Peptides
-
Receptors, Opioid, mu
-
tryptophyl-histidine
-
aspartyltyrosine
-
Morphine
-
Fentanyl