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Single-Strand DNA Binding Proteins

Single-Strand DNA Binding Proteins

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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Ruthenium(II) Polypyridyl Complexes as FRET Donors: Structure- and Sequence-Selective DNA-Binding and Anticancer

Christopher E Elgar¹, Nur Aininie Yusoh², Paul R Tiley¹

¹Department of Chemistry, Faculty of Science and Engineering, Swansea University, Swansea SA2 8PP, U.K.

Journal of the American Chemical Society

|January 6, 2023

Summary

Ruthenium(II) polypyridyl complexes (RPCs) that bind DNA can be studied using a new Förster resonance energy transfer (FRET) assay. This method reveals DNA-binding interactions and potential anticancer properties of these complexes.

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Area of Science:

Coordination Chemistry
Biophysical Chemistry
Chemical Biology

Background:

Ruthenium(II) polypyridyl complexes (RPCs) are investigated for DNA probing and anticancer applications.
These complexes emit light from metal-to-ligand charge transfer (MLCT) states.
Understanding RPC DNA interactions is crucial for developing targeted therapies.

Purpose of the Study:

To develop a novel Förster resonance energy transfer (FRET) assay for studying DNA-binding interactions of MLCT-emissive RPCs.
To characterize the binding affinities of RPCs with various DNA structures.
To explore the anticancer potential and mechanisms of action of these RPCs.

Main Methods:

Utilized FRET between MLCT-emissive RPCs and Cy5.5-labeled DNA to form mega-Stokes shift FRET pairs.
Developed a simple and rapid FRET-based binding assay.
Determined binding affinities of RPCs towards duplex, G-quadruplex, three-way junction, and mismatch DNA.

Main Results:

Established a FRET assay to quantify DNA-binding interactions of RPCs.
Derived FRET donor-acceptor proximities, offering insights into potential DNA binding sites.
Identified RPCs with encouraging anticancer properties, including synergy with PARP inhibitors.
[Ru(PIP)2(5,5'dmb)]2+ was found to inhibit DNA replication fork progression.

Conclusions:

The developed FRET assay is a simple and rapid method for assessing DNA-binding interactions of RPCs.
RPCs exhibit diverse DNA-binding affinities and potential as anticancer agents.
Mechanistic studies suggest RPCs can interfere with DNA replication, highlighting their therapeutic promise.