morphine and endomorphin-2

morphine has been researched along with endomorphin-2* in 2 studies

Other Studies

2 other study(ies) available for morphine and endomorphin-2

Article	Year
Synthesis and biological evaluations of novel endomorphin analogues containing α-hydroxy-β-phenylalanine (AHPBA) displaying mixed μ/δ opioid receptor agonist and δ opioid receptor antagonist activities. European journal of medicinal chemistry, 2015, Mar-06, Volume: 92 A novel series of endomorphin-1 (EM-1) and endomorphin-2 (EM-2) analogues was synthesized, incorporating chiral α-hydroxy-β-phenylalanine (AHPBA), and/or Dmt(1)-Tic(2) at different positions. Pharmacological activity and metabolic stability of the series was assessed. Consistent with earlier studies of β-amino acid substitution into endomorphins, multiple analogues incorporation AHPBA displayed high affinity for μ and δ opioid receptors (MOR and DOR, respectively) in radioligand competition binding assays, and an increased stability in rat brain membrane homogenates, notably Dmt-Tic-(2R,3S)AHPBA-Phe-NH2 (compound 26). Intracerebroventricular (i.c.v.) administration of 26 produced antinociception (ED50 value (and 95% confidence interval) = 1.98 (0.79-4.15) nmol, i.c.v.) in the mouse 55 °C warm-water tail-withdrawal assay, equivalent to morphine (2.35 (1.13-5.03) nmol, i.c.v.), but demonstrated DOR-selective antagonism in addition to non-selective opioid agonism. The antinociception of 26 was without locomotor activity or acute antinociceptive tolerance. This novel class of peptides adds to the potentially therapeutically relevant collection of previously reported EM analogues. Topics: Animals; CHO Cells; Cricetulus; Dihydroxyphenylalanine; Dose-Response Relationship, Drug; HEK293 Cells; Humans; Male; Mice; Mice, Inbred C57BL; Mice, Knockout; Molecular Conformation; Oligopeptides; Rats; Receptors, Opioid, delta; Receptors, Opioid, mu; Structure-Activity Relationship	2015
Endomorphin-2 with a beta-turn backbone constraint retains the potent micro-opioid receptor agonist properties. Journal of medicinal chemistry, 2008, Jan-10, Volume: 51, Issue:1 The constitutional similarity with different secondary structure preference between the Aba-Gly and the spiro-Aba-Gly scaffolds were exploited to design the novel endomorphin-2 analogs Tyr-spiro-( R/ S)-Aba-Gly-Phe-NH(2) ( 1 and 2) and Tyr-( R/ S)-Aba-Gly-Phe-NH(2) ( 3 and 4). The ( R)-spiro analog 1 was found to be a potent and selective micro-opioid agonist/partial agonist ( K (imicro) = 29.3 nM, IC(50) = 50 nM, K(e) = 0.57). NMR experiments and molecular modeling indicated that its backbone adopts mainly a beta-turn in aqueous solution. Topics: Magnetic Resonance Spectroscopy; Models, Molecular; Oligopeptides; Protein Structure, Secondary; Receptors, Opioid, mu; Solutions; Stereoisomerism; Structure-Activity Relationship	2008

Article

Year

Synthesis and biological evaluations of novel endomorphin analogues containing α-hydroxy-β-phenylalanine (AHPBA) displaying mixed μ/δ opioid receptor agonist and δ opioid receptor antagonist activities.

European journal of medicinal chemistry, 2015, Mar-06, Volume: 92

A novel series of endomorphin-1 (EM-1) and endomorphin-2 (EM-2) analogues was synthesized, incorporating chiral α-hydroxy-β-phenylalanine (AHPBA), and/or Dmt(1)-Tic(2) at different positions. Pharmacological activity and metabolic stability of the series was assessed. Consistent with earlier studies of β-amino acid substitution into endomorphins, multiple analogues incorporation AHPBA displayed high affinity for μ and δ opioid receptors (MOR and DOR, respectively) in radioligand competition binding assays, and an increased stability in rat brain membrane homogenates, notably Dmt-Tic-(2R,3S)AHPBA-Phe-NH2 (compound 26). Intracerebroventricular (i.c.v.) administration of 26 produced antinociception (ED50 value (and 95% confidence interval) = 1.98 (0.79-4.15) nmol, i.c.v.) in the mouse 55 °C warm-water tail-withdrawal assay, equivalent to morphine (2.35 (1.13-5.03) nmol, i.c.v.), but demonstrated DOR-selective antagonism in addition to non-selective opioid agonism. The antinociception of 26 was without locomotor activity or acute antinociceptive tolerance. This novel class of peptides adds to the potentially therapeutically relevant collection of previously reported EM analogues.

Topics: Animals; CHO Cells; Cricetulus; Dihydroxyphenylalanine; Dose-Response Relationship, Drug; HEK293 Cells; Humans; Male; Mice; Mice, Inbred C57BL; Mice, Knockout; Molecular Conformation; Oligopeptides; Rats; Receptors, Opioid, delta; Receptors, Opioid, mu; Structure-Activity Relationship

2015

Endomorphin-2 with a beta-turn backbone constraint retains the potent micro-opioid receptor agonist properties.

Journal of medicinal chemistry, 2008, Jan-10, Volume: 51, Issue:1

The constitutional similarity with different secondary structure preference between the Aba-Gly and the spiro-Aba-Gly scaffolds were exploited to design the novel endomorphin-2 analogs Tyr-spiro-( R/ S)-Aba-Gly-Phe-NH(2) ( 1 and 2) and Tyr-( R/ S)-Aba-Gly-Phe-NH(2) ( 3 and 4). The ( R)-spiro analog 1 was found to be a potent and selective micro-opioid agonist/partial agonist ( K (imicro) = 29.3 nM, IC(50) = 50 nM, K(e) = 0.57). NMR experiments and molecular modeling indicated that its backbone adopts mainly a beta-turn in aqueous solution.

Topics: Magnetic Resonance Spectroscopy; Models, Molecular; Oligopeptides; Protein Structure, Secondary; Receptors, Opioid, mu; Solutions; Stereoisomerism; Structure-Activity Relationship

2008