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Part Used : ผลActivity : CYP1A2 INHIBITIONSolvent/Active Compound : PiperlonguminineType of experiment : in vitroType of animal : -Type of study : -N(Total) : -N(Treatment) : -Sex : -Age : -Route : -Dose/Conc.(herb) : 0-100 micromolarDuration : -Type of interaction : PharmacokineticsInteraction with drug : Phenacetin*/AcetophenetidinDose/Conc.(drug) : 80 micromolarResult : PositiveRemark : Piperlonguminine (PL) strongly inhibited CYP1A2-mediated phenacetin O-deethylation with an lC50 value of 8.8 micromolar. PL strongly and concentration-dependently inhibited only CYP1A2- catalyzed phenacetin O-deethylation. However, other CYPs were not inhibited significantly.
Part Used : ผลActivity : CYP1A1 INHIBITIONSolvent/Active Compound : PiperlonguminineType of experiment : in vitroType of animal : -Type of study : -N(Total) : -N(Treatment) : -Sex : -Age : -Route : -Dose/Conc.(herb) : 0-40 micromolarDuration : -Type of interaction : PharmacokineticsInteraction with drug : Phenacetin*/AcetophenetidinDose/Conc.(drug) : 20-80 micromolarResult : NegativeRemark : Piperlonguminine (PL) only decreased CYP 1A2-catalyzed phenacetin O-deethylase activity with lC50 values of 10.0 micromolar, whereas the lC50 of PL on CYP1A1-actalyzed phenacetion O-deethylase activity was fivefold higher than the value of CYP1A2. Accordingly, PL was a specific substrate having inhibitiory effects on the CYP1A2 in HLMs, not CYP1A1.
Part Used : ผลActivity : CYP1A2 INHIBITIONSolvent/Active Compound : PiperlonguminineType of experiment : in vitroType of animal : -Type of study : -N(Total) : -N(Treatment) : -Sex : -Age : -Route : -Dose/Conc.(herb) : 0-40 micromolarDuration : -Type of interaction : PharmacokineticsInteraction with drug : Phenacetin*/AcetophenetidinDose/Conc.(drug) : 20-80 micromolarResult : PositiveRemark : The inhibition mechanism was divided into two separate modes based on the Piperlonguminine (PL) concentration in HLMs. At low concentrations (0-16 micromolar; approximately 0.5x, 1x and 2x of lC50), PL was a reversible competitive inhibitor and the Ki value was calculated from a secondary plot with a Ki value of 1.39 micromolar. At high concentrations (16-40 micromolar; approximately as 2x and 5x of lC50), PL was an uncompetitive inhibitor.
