AZ505 ditrifluoroacetate demonstrates high selectivity and activity at submicromolar concentrations in vitro. The IC50 of AZ505 ditrifluoroacetate against SMYD2 is 0.12 μM, which is >600-fold higher than its IC50 values against other histone methyltransferases, including SMYD3 (IC50>83.3 μM), DOT1L (IC50>83.3 μM), and EZH2 (IC50>83.3 μM) [1]. AZ505 ditrifluoroacetate functions as a potent and selective inhibitor of SMYD2, with an IC50 of 0.12 μM. The human SMYD (SET and MYND domain-containing protein) family encompasses five members (SMYD1-5). Furthermore, AZ505 ditrifluoroacetate does not inhibit the enzymatic activities of a panel of protein lysine methyltransferases. It is slated for an isothermal titration calorimetry (ITC) binding study, with a Kd of 0.5 μM. In contrast, the calculated Kd for the p53 substrate peptide is 3.7 μM. The binding of AZ505 ditrifluoroacetate to SMYD2 is primarily driven by entropy, indicative of hydrophobic interactions with limited specific hydrogen bonding [2].
体外研究
AZ505 ditrifluoroacetate demonstrates high selectivity and activity at submicromolar concentrations in vitro. The IC50 of AZ505 ditrifluoroacetate against SMYD2 is 0.12 μM, which is >600-fold higher than its IC50 values against other histone methyltransferases, including SMYD3 (IC50>83.3 μM), DOT1L (IC50>83.3 μM), and EZH2 (IC50>83.3 μM) [1].
AZ505 ditrifluoroacetate functions as a potent and selective inhibitor of SMYD2, with an IC50 of 0.12 μM. The human SMYD (SET and MYND domain-containing protein) family encompasses five members (SMYD1-5). Furthermore, AZ505 ditrifluoroacetate does not inhibit the enzymatic activities of a panel of protein lysine methyltransferases. It is slated for an isothermal titration calorimetry (ITC) binding study, with a Kd of 0.5 μM. In contrast, the calculated Kd for the p53 substrate peptide is 3.7 μM. The binding of AZ505 ditrifluoroacetate to SMYD2 is primarily driven by entropy, indicative of hydrophobic interactions with limited specific hydrogen bonding [2].
搜索
