Compounds > enkephalin--leucine-2-alanine

enkephalin--leucine-2-alanine and 1-pyrenylalanine

enkephalin--leucine-2-alanine has been researched along with 1-pyrenylalanine* in 1 studies

Other Studies

1 other study(ies) available for enkephalin--leucine-2-alanine and 1-pyrenylalanine

Article	Year
Tyr1-substituted and fluorescent Pya1-enkephalins bind strongly and selectively to mu and delta opiate receptors. Biochemical and biophysical research communications, 1986, May-14, Volume: 136, Issue:3 The fluorescent enkephalins in which an essential Tyr1 residue is replaced by L-1-pyrenylalanine (Pya) were synthesized and examined in the receptor binding assays. [Pya1, Leu5]Enkephalin and its methyl ester showed binding characteristics specific for the opiate receptors, exhibiting a potent inhibition of Tyr1-containing enkephalins. Surprisingly, the methyl ester displayed almost the same potencies to those of DAGO-enkephalin. This analog bound 24-fold more strongly to mu than to delta-receptors. C-terminal free analog Pya1-Enk-OH was delta-preferential with a fairly good affinity. These results indicate that Tyr1 in enkephalin is not necessary to recognition of the opiate receptors. Topics: Alanine; Animals; Binding, Competitive; Crystallography; Enkephalin, Ala(2)-MePhe(4)-Gly(5)-; Enkephalin, Leucine; Enkephalin, Leucine-2-Alanine; Enkephalins; Guinea Pigs; Ileum; Pyrenes; Receptors, Opioid; Receptors, Opioid, delta; Receptors, Opioid, mu; Spectrometry, Fluorescence; Structure-Activity Relationship; Tyrosine	1986

Article

Year

Tyr1-substituted and fluorescent Pya1-enkephalins bind strongly and selectively to mu and delta opiate receptors.

Biochemical and biophysical research communications, 1986, May-14, Volume: 136, Issue:3

The fluorescent enkephalins in which an essential Tyr1 residue is replaced by L-1-pyrenylalanine (Pya) were synthesized and examined in the receptor binding assays. [Pya1, Leu5]Enkephalin and its methyl ester showed binding characteristics specific for the opiate receptors, exhibiting a potent inhibition of Tyr1-containing enkephalins. Surprisingly, the methyl ester displayed almost the same potencies to those of DAGO-enkephalin. This analog bound 24-fold more strongly to mu than to delta-receptors. C-terminal free analog Pya1-Enk-OH was delta-preferential with a fairly good affinity. These results indicate that Tyr1 in enkephalin is not necessary to recognition of the opiate receptors.

Topics: Alanine; Animals; Binding, Competitive; Crystallography; Enkephalin, Ala(2)-MePhe(4)-Gly(5)-; Enkephalin, Leucine; Enkephalin, Leucine-2-Alanine; Enkephalins; Guinea Pigs; Ileum; Pyrenes; Receptors, Opioid; Receptors, Opioid, delta; Receptors, Opioid, mu; Spectrometry, Fluorescence; Structure-Activity Relationship; Tyrosine

1986