Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, Arkansas 72205-7199, United States.
ACS Chem Biol. 2013 Aug 16;8(8):1722-9. doi: 10.1021/cb400305r. Epub 2013 May 28.
Using a robust and quantitative assay, we have identified a novel class of DNA polymerase inhibitors that exhibits some specificity against an enzyme involved in resistance to anti-cancer drugs, namely, human DNA polymerase eta (hpol η). In our initial screen, we identified the indole thiobarbituric acid (ITBA) derivative 5-((1-(2-bromobenzoyl)-5-chloro-1H-indol-3-yl)methylene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione (ITBA-12) as an inhibitor of the Y-family DNA member hpol η, an enzyme that has been associated with increased resistance to cisplatin and doxorubicin treatments. An additional seven DNA polymerases from different subfamilies were tested for inhibition by ITBA-12. Hpol η was the most potently inhibited enzyme (30 ± 3 μM), with hpol β, hpol γ, and hpol κ exhibiting comparable but higher IC50 values of 41 ± 24, 49 ± 6, and 59 ± 11 μM, respectively. The other polymerases tested had IC50 values closer to 80 μM. Steady-state kinetic analysis was used to investigate the mechanism of polymerase inhibition by ITBA-12. Based on changes in the Michaelis constant, it was determined that ITBA-12 acts as an allosteric (or partial) competitive inhibitor of dNTP binding. The parent ITBA scaffold was modified to produce 20 derivatives and establish structure-activity relationships by testing for inhibition of hpol η. Two compounds with N-naphthoyl Ar-substituents, ITBA-16 and ITBA-19, were both found to have improved potency against hpol η with IC50 values of 16 ± 3 μM and 17 ± 3 μM, respectively. Moreover, the specificity of ITBA-16 was improved relative to that of ITBA-12. The presence of a chloro substituent at position 5 on the indole ring appears to be crucial for effective inhibition of hpol η, with the indole N-1-naphthoyl and N-2-naphthoyl analogues being the most potent inhibitors of hpol η. These results provide a framework from which second-generation ITBA derivatives may be developed against specialized polymerases that are involved in mechanisms of radio- and chemo-resistance.
利用一种强大且定量的检测方法,我们发现了一类新型的 DNA 聚合酶抑制剂,该抑制剂对一种与抗癌药物耐药性相关的酶,即人类 DNA 聚合酶 eta(hpol η)具有一定的特异性。在我们的初步筛选中,我们鉴定出吲哚硫代巴比妥酸(ITBA)衍生物 5-((1-(2-溴苯甲酰基)-5-氯-1H-吲哚-3-基)亚甲基)-2-硫代二氢嘧啶-4,6(1H,5H)-二酮(ITBA-12)是 Y 家族 DNA 成员 hpol η 的抑制剂,该酶与顺铂和阿霉素治疗的耐药性增加有关。我们还测试了来自不同亚家族的另外七种 DNA 聚合酶是否受到 ITBA-12 的抑制。hpol η 是被抑制得最强烈的酶(30 ± 3 μM),hpol β、hpol γ 和 hpol κ 的抑制 IC50 值相当,但更高,分别为 41 ± 24、49 ± 6 和 59 ± 11 μM。其余测试的聚合酶的 IC50 值更接近 80 μM。我们使用稳态动力学分析来研究 ITBA-12 对聚合酶抑制的作用机制。根据米氏常数的变化,确定 ITBA-12 作为 dNTP 结合的别构(或部分)竞争性抑制剂。我们对 ITBA 母体结构进行了修饰,生成了 20 个衍生物,并通过测试其对 hpol η 的抑制作用来建立结构-活性关系。两个具有 N-萘酰基 Ar-取代基的化合物 ITBA-16 和 ITBA-19 均被发现对 hpol η 的抑制作用更强,IC50 值分别为 16 ± 3 μM 和 17 ± 3 μM。此外,ITBA-16 的特异性相对于 ITBA-12 有所提高。吲哚环 5 位上的氯取代基似乎对 hpol η 的有效抑制至关重要,带有吲哚 N-1-萘酰基和 N-2-萘酰基的类似物是 hpol η 的最强抑制剂。这些结果为开发针对涉及放射和化学耐药性机制的特殊聚合酶的第二代 ITBA 衍生物提供了框架。