Design of an Aptamer-Amphiphile for the Detection of β-Lactoglobulin on a Liquid Crystal Interface

Ana Paula Brumann Clemente, Huihui Kuang, Ahmed M. Shabana, Theodore P. Labuza, Efrosini Kokkoli

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)2763-2770
Number of pages8
JournalBioconjugate Chemistry
Volume30
Issue number11
DOIs
StatePublished - Nov 20 2019

Bibliographical note

Funding Information:
A.P.B.C. was supported by a scholarship from the Brazil Scientific Mobility Program (CAPES). This work was partially supported by University of Minnesota’s MnDRIVE program. Parts of this work were carried out in the University of Minnesota Characterization Facility, which receives partial support from NSF through the MRSEC program.

Publisher Copyright:
© 2019 American Chemical Society.

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