Stapled α‐helical RIR (Rev1‐interacting region) peptides of DNA POL κ bind more effectively to the RIR‐interface of the C‐terminal recruitment domain of the translesion synthesis DNA polymerase Rev1 than unstapled peptide. The tightest‐binding stapled peptide translocates into cells and enhances the cytotoxicity of DNA damaging agents while reducing mutagenesis. Drugs with these characteristics could potentially serve as adjuvants to improve chemotherapy and reduce acquired resistance by inhibiting Rev1‐dependent mutagenic translesion synthesis.

中文翻译：

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钉合的 POL κ 肽靶向 REV1 以抑制诱变的跨损伤合成。

DNA POL κ 的钉合α-螺旋 RIR（Rev1 相互作用区）肽比未钉合肽更有效地与跨损伤合成 DNA 聚合酶 Rev1 的 C 端募集结构域的 RIR 界面结合。结合最紧密的订书肽易位进入细胞并增强 DNA 损伤剂的细胞毒性，同时减少诱变。具有这些特征的药物可能作为佐剂，通过抑制 Rev1 依赖性诱变跨病变合成来改善化疗和降低获得性耐药。