p-Ethynylphenylalanine (4-Ethynyl-L-phenylalanine) is a potent, selective, reversible, and competitive inhibitor of tryptophan hydroxylase (TPH), displaying a Ki value of 32.6 μM. This inhibition directly impacts the biosynthesis pathway of serotonin, effectively reducing its production[1].
体内研究
When administered intraperitoneally at a dose of 30 mg/kg, it leads to a reduction in levels of serotonin (5-HT) and its metabolite 5-HIAA in the rat midbrain, highlighting its impact on serotonin metabolism without affecting other tissues[1].
Moreover, p-Ethynylphenylalanine does not interfere with the activity of aromatic amino acid decarboxylase, further specifying its targeted inhibitory effect on the serotonin synthesis pathway[1].
体外研究
In addition to its biochemical role, p-Ethynylphenylalanine is valuable in click chemistry due to its alkyne group. This functional group enables it to participate in copper-catalyzed azide-alkyne cycloaddition (CuAAc) reactions, allowing for the conjugation with azide-containing molecules. Its inhibition of serotonin biosynthesis is both selective and reversible, underscoring its potential as a tool for studying serotonin's physiological and pathological roles[1].
Despite its efficacy in inhibiting TPH, p-Ethynylphenylalanine exhibits low affinity towards various recombinant 5-HT receptors, including 5-HT1, 5-HT2, 5-HT4, 5-HT5, 5-HT6, and 5-HT7, indicating specificity in its mode of action[1].
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