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1.
Article in English | MEDLINE | ID: mdl-37969927

ABSTRACT

The introduction of the in-vitro evolution method known as SELEX (Systematic Evolution of Ligands by Exponential enrichment) more than 30 years ago led to the conception of versatile synthetic receptors known as aptamers. Offering many benefits such as low cost, high stability and flexibility, aptamers have sparked innovation in molecular diagnostics, enabled advances in synthetic biology and have facilitated new therapeutic approaches. The SELEX method itself is inherently adaptable and offers near limitless possibilities in yielding functional nucleic acid ligands. This Primer serves to provide guidance on experimental design and highlight new growth areas for this impactful technology.

2.
Bioconjug Chem ; 27(6): 1493-9, 2016 06 15.
Article in English | MEDLINE | ID: mdl-27115292

ABSTRACT

A pH-driven DNA nanomachine based on the human α-thrombin binding aptamer was designed for the specific catch-and-release of human α-thrombin at neutral and acidic pH, respectively. In neutral conditions, the thrombin aptamer component of the nanomachine is exposed and exists in the G-quadruplex conformation required to bind to the target protein. At slightly acidic pH, the polyadenine tail of the nanomachine becomes partially protonated and A+(anti)•G(syn) mispairing results in a conformational change, causing the target protein to be released. Förster resonance energy transfer (FRET) was used to monitor conformational switching over multiple pH cycles. Electrophoretic mobility shift assay (EMSA) and fluorescence anisotropy were used to show pH dependent protein binding and release by the nanomachine. This approach could be applied generally to existing G-rich aptamers to develop novel biosensors, theranostics, and nanoswitches.


Subject(s)
Aptamers, Nucleotide/metabolism , Thrombin/metabolism , Aptamers, Nucleotide/chemistry , Aptamers, Nucleotide/genetics , Base Sequence , Drug Design , Humans , Hydrogen-Ion Concentration , Models, Molecular , Nucleic Acid Conformation , Protein Binding , Protein Conformation , Spectrometry, Fluorescence , Thrombin/chemistry
3.
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