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Related Concept Videos

Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

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For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
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Related Experiment Video

Updated: May 22, 2025

Author Spotlight: Advancements in DNA Nanosensors &#8211; Addressing Sensitivity and Selectivity Challenges in Molecular Detection
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Switching on Supramolecular DNA Junction Binding Using a Human Enzyme.

Subhendu Karmakar1, Samuel J Dettmer1, Catherine A J Hooper1

  • 1School of Chemistry, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK.

Angewandte Chemie (International Ed. in English)
|March 15, 2025
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel metallo-supramolecular cylinder that binds non-canonical DNA junctions only when activated by the enzyme NAD(P)H:quinone oxidoreductase 1 (NQO1) and its cofactor NADPH.

Keywords:
Bio‐inorganicDNA three‐way junctionsDNA‐recognitionEnzyme‐mediated activationMetallo‐supramolecular chemistry

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Area of Science:

  • Supramolecular Chemistry
  • Chemical Biology
  • Biotechnology

Background:

  • Non-canonical DNA structures are crucial in human diseases and nucleic acid nanoscience.
  • Controlling the binding and modulation of these DNA structures is an area of active research.
  • Developing targeted binding agents for specific DNA structures is a key challenge.

Purpose of the Study:

  • To design a metallo-supramolecular agent capable of binding non-canonical DNA junctions.
  • To achieve enzyme-activated, "on-command" control over DNA junction binding.
  • To establish a system with NAND logic control based on enzyme presence and cofactor availability.

Main Methods:

  • Development of a metallo-supramolecular triple-helicate cylinder with enzyme-cleavable arms.
  • Utilizing NAD(P)H:quinone oxidoreductase 1 (NQO1) and nicotinamide adenine dinucleotide phosphate (NADPH) for activation.
  • Employing computational modeling to understand binding activation mechanisms.

Main Results:

  • An inert metallo-supramolecular cylinder was engineered, which becomes active upon enzymatic reduction.
  • Enzyme-mediated removal of six terminal quinone-bearing arms transforms the cylinder into a DNA junction-binding agent.
  • The system demonstrated NAND logic control, activating binding in response to NQO1, NADPH, and the absence of an inhibitor.
  • Computational analysis suggested conformational flexibility changes, rather than steric unblocking, drive binding activation.

Conclusions:

  • A novel enzyme-activated supramolecular system for controlling DNA junction binding has been developed.
  • This system offers precise "on-command" control, responding to specific biological stimuli.
  • The findings provide a foundation for designing sophisticated, inert supramolecular structures that can be activated by enzymes for diverse applications.