説明:
(abstract)Certain DNA aptamers can serve as effective inhibitors, although their inhibitory action is typically unidirectional. Simple removal of these aptamers from their target complexes could improve their application in areas such as oligonucleotide therapeutics. In the current study, we used uracilDNA glycosylase from Mycobacterium smegmatis (UdgX), which binds covalently to DNA after uracil removal. A suitable site for incorporating uracil-DNA into a G-quadruplex-structured DNA aptamer was identified, and subsequent restoration of thrombin activity previously inhibited by the DNA aptamers was examined. The addition of UdgX restored thrombin activity to nearly 100% within 1 min, demonstrating greater speed and efficacy than complementary strand addition targeting the thrombin aptamer. Furthermore, UdgX restored the binding capacity of the anti-VEGF antibody bevacizumab that had been inhibited by a hairpin-structured aptamer. These findings highlight the versatile potential of UdgX to turn on protein functions inhibited by DNA aptamers.
権利情報:
キーワード: Anticoagulant, aptamer, aptamer remover, UdgX, uracil-DNA glycosylase
刊行年月日: 2026-04-15
出版者: American Chemical Society (ACS)
掲載誌:
研究助成金:
原稿種別: 出版者版 (Version of record)
MDR DOI:
公開URL: https://doi.org/10.1021/acsnanoscienceau.5c00143
関連資料:
その他の識別子:
連絡先:
更新時刻: 2026-06-25 09:39:07 +0900
MDRでの公開時刻: 2026-06-25 12:26:54 +0900
| ファイル名 | サイズ | |||
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Turning on Protein Function Inhibi-2026-Kanazu.pdf
(サムネイル)
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サイズ | 4.56MB | 詳細 |
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Turning on Protein Function Inhibi-2026-Kanaz1.pdf
application/pdf |
サイズ | 1.2MB | 詳細 |