An aptamer-amphiphile
was designed that binds to β-lactoglobulin
(β-LG), a major allergen from cow’s milk. For this work,
a 23-nucleotide ssDNA aptamer β-LG-23, capable of forming antiparallel
G-quadruplexes was used, and its specificity and binding affinity
of 22 ± 2 nM for β-LG were evaluated via enzyme-linked
apta-sorbent assay (ELASA). The β-LG-23 aptamer was synthesized
as an amphiphile by conjugating it to a C16 double tail
via different spacers, and the effect of the spacers on the binding
affinity and secondary structure of the aptamer was investigated.
From all amphiphiles tested, direct conjugation of the aptamer to
the tail gave the lowest binding affinity to β-LG (37 ±
2 nM), while maintaining the antiparallel G-quadruplex secondary structure
of the aptamer. As a proof of concept, the β-LG-23 aptamer-amphiphile
was used to decorate the interface of a liquid crystal (LC) and effectively
detected 10 nM or 0.18 ppm of β-LG with a 20 min equilibration
time, thus demonstrating that it has the potential to be used for
fast and label-free detection of β-LG.
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