Probing and regulating the activity of cellular enzymes by using DNA tetrahedron nanostructures

Abstract

Given the essential role of apurinic/apyrimidinic endonuclease (APE1) in gene repair and cancer progression, we report a novel approach for probing and regulating cellular APE1 activity by using DNA tetrahedrons.

Accurate cancer cell identification and microRNA silencing induced therapy using tailored DNA tetrahedron nanostructures

“…DNA tetrahedron nanostructures have attracted enormous interest owing to their unique advantages, such as ease of self-assembly, excellent biocompatibility, high nuclease stability, remarkable transmembrane capability through a caveolin-dependent pathway and availability for multiple modications. [15][16][17][18] To signicantly improve the survival rate of cancer patients, besides accurate cancer identication, an efficient treatment strategy is another crucial step. Gene silencing as a kind of gene therapy has now been considered as one of the most promising options to overcome the limitations of traditional cancer therapy.…”

High‐Fidelity Determination and Tracing of Small Extracellular Vesicle Cargoes

“…For the cell model, the optimal incubation time was determined by continuously measuring the fluorescence images after introducing either the quencher‐free fLIGHT probe or a single‐stranded molecular probe (without quencher) into A549 cells. [ 31 ] Briefly, A549 cells were planted and cultured on 15 mm glass‐bottom dishes to a moderate concentration. The cultured medium was discarded and it was replaced with a fresh medium (100 µL), followed by pipetting fLIGHT solution or single‐stranded molecular probe solution at the same final concentration (1 × 10 −6 m ).…”

Recent Advances of DNA Tetrahedra for Therapeutic Delivery and Biosensing

“…Zhang et al. recently constructed a TDN with an antenna‐like dsDNA containing a fluorophore, quencher and apurinic/apyrimidinic (AP) site for the highly sensitive detection of cytoplasmic AP endonuclease (APE1) in living cells [50] . Incorporation of the AP site on the TDN scaffold displayed increased binding affinity of APE1 but diminished its catalytic activity effectively making it an APE1 inhibitor.…”