Switching on Supramolecular DNA Junction Binding Using a Human Enzyme.

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Tác giả: Samuel J Dettmer, Michael J Hannon, Nikolas J Hodges, Catherine A J Hooper, Subhendu Karmakar

Ngôn ngữ: eng

Ký hiệu phân loại: 796.35722 Ball games

Thông tin xuất bản: Germany : Angewandte Chemie (International ed. in English) , 2025

Mô tả vật lý:

Bộ sưu tập: NCBI

ID: 742481

Non-canonical DNA junction structures are important in human disease and in nucleic acid nanoscience and there is a growing interest in how to bind and modulate them. A key next step is to exert "on command" control over such binding. Herein we develop a new metallo-supramolecular triple-helicate cylinder agent that is inert to DNA junction binding until activated by human enzyme NAD(P)H:quinone oxidoreductase 1 (NQO1) and its cofactor nicotinamide adenine dinucleotide phosphate (NADPH). This inactive cylinder bears six flexible arms each with a quinone group at the termini. Reduction by the enzyme leads to all six arms being removed, transforming the inert cylinder into a new and active metallo-supramolecular agent that binds junctions. This gives the ability to "switch-on" DNA junction formation and binding in response to the presence of two external stimuli - a human enzyme overexpressed in many disease states, and NADPH - and absence of inhibitor, giving NAND logic control. Modelling indicates the binding activation originates not in steric unblocking but changes in conformational flexibility. The work provides the foundation for and a route map toward future designs of sophisticated, inert, and supramolecular structures which are transformed by enzymes into new, active, and supramolecular structures for a variety of potential applications.
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