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¹ Department of Applied Biological Science, Tokyo University of Science, Noda, Chiba, Japan
² Department of Nutritional Science, Kobe-Gakuin University, Kobe, Hyogo, Japan
³ Faculty of Pharmaceutical Sciences, Tokyo University of Science, Noda, Chiba, Japan
⁴ Frontier Research Center for Genome and Drug Discovery, Tokyo University of Science, Noda, Chiba, Japan
⁵ High Technology Research Center, Kobe-Gakuin University, Kobe, Hyogo, Japan

We previously reported that phenolic compounds, petasiphenol and curcumin (diferuloylmethane), were a selective inhibitor of DNA polymerase (pol ) in vitro. The purpose of this study was to investigate the molecular structural relationship of curcumin and 13 chemically synthesized derivatives of curcumin. The inhibitory effect on pol (full-length, i.e. intact pol including the BRCA1 C- terminal [BRCT] domain) by some derivatives was stronger than that by curcumin, and monoacetylcurcumin (compound 13) was the strongest pol inhibitor of all the compounds tested, achieving 50% inhibition at a concentration of 3.9 µM. The compound did not influence the activities of replicative pols such as , , and . It had no effect on pol ß activity either, although the three-dimensional structure of pol ß is thought to be highly similar to that of pol . Compound 13 did not inhibit the activity of the C-terminal catalytic domain of pol including the pol ß-like core, in which the BRCT motif was deleted from its N-terminal region. MALDI-TOF MS analysis demonstrated that compound 13 bound selectively to the N-terminal domain of pol , but did not bind to the C-terminal region. Based on these results, the pol -inhibitory mechanism of compound 13 is discussed.

^* Correspondence: E-mail: mizushin{at}nutr.kobegakuin.ac.jp

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