Design of an Aptamer-Amphiphile for the Detection of ß-Lactoglobulin on a Liquid Crystal Interface.
Bioconjug Chem
; 30(11): 2763-2770, 2019 11 20.
Article
en En
| MEDLINE
| ID: mdl-31589417
ABSTRACT
An aptamer-amphiphile was designed that binds to ß-lactoglobulin (ß-LG), a major allergen from cow's milk. For this work, a 23-nucleotide ssDNA aptamer ß-LG-23, capable of forming antiparallel G-quadruplexes was used, and its specificity and binding affinity of 22 ± 2 nM for ß-LG were evaluated via enzyme-linked apta-sorbent assay (ELASA). The ß-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 ß-LG (37 ± 2 nM), while maintaining the antiparallel G-quadruplex secondary structure of the aptamer. As a proof of concept, the ß-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 ß-LG with a 20 min equilibration time, thus demonstrating that it has the potential to be used for fast and label-free detection of ß-LG.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
ADN de Cadena Simple
/
Diseño de Fármacos
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Aptámeros de Nucleótidos
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Cristales Líquidos
/
Lactoglobulinas
Tipo de estudio:
Diagnostic_studies
Límite:
Animals
Idioma:
En
Revista:
Bioconjug Chem
Asunto de la revista:
BIOQUIMICA
Año:
2019
Tipo del documento:
Article
País de afiliación:
Estados Unidos