Probing the interaction of copper cofactor and azachalcone substrate with G-quadruplex of DNA based Diels-Alderase by site-specific fluorescence quenching titration
文献类型：期刊论文
| 作者 | Cheng, Mingpan1,2; Hao, Jingya1,2; Li, Yinghao2; Cheng, Yu1,2; Jia, Guoqing2; Zhou, Jun3; Li, Can2 |
| 刊名 | BIOCHIMIE
 |
| 出版日期 | 2018-03-01 |
| 卷号 | 146页码:20-27 |
| 关键词 | Dnazyme G-quadruplex G-quadruplex Ligand Fluorescence Diels-alder Asymmetric Catalysis |
| ISSN号 | 0300-9084 |
| DOI | 10.1016/j.biochi.2017.11.001 |
| 文献子类 | Article |
| 英文摘要 | DNAzymes have been widely used in biosensors, asymmetric synthesis and pharmaceuticals. Typically, metal cofactor and substrate interact with DNA by supramolecular interactions in DNAzyme based asymmetric catalysis. However, binding positions of cofactor and substrate with DNA scaffold are not well understood, which is an obstacle to reveal the assembly and catalysis mechanisms of DNAzyme. Herein, we report a method of site-specific fluorescence quenching titration to elucidate the assembly and catalysis processes of a G-quadruplex based Diels-Alderase DNAzyme. Titration data indicate that cofactor Cu(II)-terpyridine stacked atop 5' and 3' external G-quartets with high and low binding affinities respectively, and induced the G-quadruplex to form a hybrid-1 topology. Substrate azachalcone interacted with 3' quartet exclusively, implicating that asymmetric Diels-Alder cycloaddition may occur at 3' G-quartet. In addition, enzyme kinetic analyses show that activity and enantioselectivity of the DNAzyme were substantially preserved after attaching the fluorophores. Overall, site-specific fluorescence quenching is a concise and efficient approach to probe the assembly processes of DNAzyme. (c) 2017 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved. |
| WOS关键词 | TELOMERIC G-QUADRUPLEX ; ASYMMETRIC CATALYSIS ; MICHAEL ADDITION ; ACTIVE-SITE ; K+ SOLUTION ; CIRCULAR-DICHROISM ; RATE ACCELERATION ; HYBRID CATALYSTS ; RATIONAL DESIGN ; LIGAND-BINDING |
| WOS研究方向 | Biochemistry & Molecular Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000425283600003 |
| 出版者 | ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER |
| 源URL | [http://cas-ir.dicp.ac.cn/handle/321008/168854]  |
| 专题 | 大连化学物理研究所_中国科学院大连化学物理研究所 |
| 通讯作者 | Li, Can |
| 作者单位 | 1.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 2.Chinese Acad Sci, Dalian Inst Chem Phys, State Key Lab Catalysis, Dalian 116023, Peoples R China 3.Nanjing Univ, Sch Chem Chem Engn, State Key Lab Analyt Chem Life Sci, Nanjing 210023, Jiangsu, Peoples R China |
| 推荐引用方式 GB/T 7714 | Cheng, Mingpan,Hao, Jingya,Li, Yinghao,et al. Probing the interaction of copper cofactor and azachalcone substrate with G-quadruplex of DNA based Diels-Alderase by site-specific fluorescence quenching titration[J]. BIOCHIMIE,2018,146:20-27. |
| APA | Cheng, Mingpan.,Hao, Jingya.,Li, Yinghao.,Cheng, Yu.,Jia, Guoqing.,...&Li, Can.(2018).Probing the interaction of copper cofactor and azachalcone substrate with G-quadruplex of DNA based Diels-Alderase by site-specific fluorescence quenching titration.BIOCHIMIE,146,20-27. |
| MLA | Cheng, Mingpan,et al."Probing the interaction of copper cofactor and azachalcone substrate with G-quadruplex of DNA based Diels-Alderase by site-specific fluorescence quenching titration".BIOCHIMIE 146(2018):20-27. |
入库方式： OAI收割
来源：大连化学物理研究所
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