PF-02929366 is an allosteric inhibitor of methionine adenosyltransferase 2A (MAT2A), which converts methionine and ATP into S-adenosylmethionine (SAM). This metabolite supplies methyl groups for reactions involving proteins, DNA and RNA.
The PF-02929366 chemical structure contains a chlorinated triazoloquinoline core, a phenyl substituent and a dimethylaminoethyl side chain. Its molecular formula is C20H19ClN4.
Application of PF-02929366
The same compound is studied as the PF-9366 MAT2A inhibitor to investigate how SAM availability influences methylation and cell growth. Measuring SAM alongside methylation markers and proliferation helps distinguish metabolic effects from downstream growth responses.
The compound also supports comparisons between pharmacological inhibition and genetic manipulation of MAT2A or its regulatory partner, MAT2B. Treatment duration matters because cells can respond to inhibition by increasing MAT2A expression.
In Vitro
The PF-02929366 MAT2A inhibitor has a reported Kd of 170 nM and biochemical IC50 of 420 nM. These describe binding affinity and functional inhibition, respectively, and should not be treated as interchangeable measures.
In H520 lung carcinoma cells, SAM production was inhibited with an IC50 of 1.2 µM, and compensatory MAT2A upregulation was reported. Measuring enzyme abundance during longer treatments helps assess adaptation rather than assuming that initial inhibition remains constant.
For stock calculations, the PF-02929366 molecular weight is 350.84 g/mol. Solvent compatibility and precipitation after dilution should be checked against batch documentation.
In Vivo
A 2021 study reported reduced tumour growth in a breast cancer patient-derived xenograft model treated with PF-9366 at 50 mg/kg.
The result remains specific to that model. Supplier formulation examples alone do not establish exposure, tolerability or an appropriate dosing schedule for another study.
Biochemical and Physiological Actions
Crystallographic analysis of the PF-02929366 molecular structure in complex with MAT2A identified an allosteric site overlapping the MAT2B-binding interface. Binding alters the catalytic site without occupying the substrate pocket.
The original kinetic analysis reported increased substrate affinity alongside reduced enzyme turnover. Consequently, stronger substrate binding does not imply faster SAM production. Lower SAM availability can affect downstream methylation, but the compound should not be described as a direct inhibitor of every SAM-dependent methyltransferase.
Features and Benefits of PF-02929366
The PF-02929366 structure has been characterised in target-binding studies, supporting its use as an allosteric reference compound. Separate affinity, enzyme and cellular measurements provide complementary evidence rather than a single universal potency value.
Match CAS 72882-78-1 and the structural record when comparing material under the two code names. Analytical identity and batch documentation remain relevant when relating a purchased sample to published experiments.
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