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Selection and Characterization of DNA Aptamers for Egg White Lysozyme

We have selected aptamers binding to lysozyme from a DNA library using capillary electrophoresis-systematic evolution of ligands by exponential enrichment. During the selection process the dissociation constant of the ssDNA pool decreased from the micromolar to the low nanomolar range within five ro...

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Detalles Bibliográficos
Autores principales: Tran, Dinh T., Janssen, Kris P. F., Pollet, Jeroen, Lammertyn, Elke, Anné, Jozef, Van Schepdael, Ann, Lammertyn, Jeroen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6257241/
https://www.ncbi.nlm.nih.gov/pubmed/20335968
http://dx.doi.org/10.3390/molecules15031127
Descripción
Sumario:We have selected aptamers binding to lysozyme from a DNA library using capillary electrophoresis-systematic evolution of ligands by exponential enrichment. During the selection process the dissociation constant of the ssDNA pool decreased from the micromolar to the low nanomolar range within five rounds of selection. The final aptamer had a dissociation constant of 2.8 ± 0.3 nM, 6.1 ± 0.5 nM, and 52.9 ± 9.1 nM as determined by fluorescence anisotropy, surface plasmon resonance and affinity capillary electrophoresis respectively. The aptamers were successfully challenged for specificity against other egg white proteins. The high affinity aptamers open up possibilities for the development of aptamer based food and medical diagnostics.