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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MDPI AG
2010-03-01
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Series: | Molecules |
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Online Access: | http://www.mdpi.com/1420-3049/15/3/1127/ |
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author | Jeroen Lammertyn Ann Van Schepdael Jozef Anné Elke Lammertyn Jeroen Pollet Kris P. F. Janssen Dinh T. Tran |
author_facet | Jeroen Lammertyn Ann Van Schepdael Jozef Anné Elke Lammertyn Jeroen Pollet Kris P. F. Janssen Dinh T. Tran |
author_sort | Jeroen Lammertyn |
collection | DOAJ |
description | 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. |
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id | doaj.art-c6e818c8b03e412ba214c54165d97d50 |
institution | Directory Open Access Journal |
issn | 1420-3049 |
language | English |
last_indexed | 2024-04-13T03:17:56Z |
publishDate | 2010-03-01 |
publisher | MDPI AG |
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series | Molecules |
spelling | doaj.art-c6e818c8b03e412ba214c54165d97d502022-12-22T03:04:52ZengMDPI AGMolecules1420-30492010-03-011531127114010.3390/molecules15031127Selection and Characterization of DNA Aptamers for Egg White LysozymeJeroen LammertynAnn Van SchepdaelJozef AnnéElke LammertynJeroen PolletKris P. F. JanssenDinh T. TranWe 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.http://www.mdpi.com/1420-3049/15/3/1127/aptamercapillary electrophoresisfood allergenlysozymesystematic evolution of ligands by exponential enrichment |
spellingShingle | Jeroen Lammertyn Ann Van Schepdael Jozef Anné Elke Lammertyn Jeroen Pollet Kris P. F. Janssen Dinh T. Tran Selection and Characterization of DNA Aptamers for Egg White Lysozyme Molecules aptamer capillary electrophoresis food allergen lysozyme systematic evolution of ligands by exponential enrichment |
title | Selection and Characterization of DNA Aptamers for Egg White Lysozyme |
title_full | Selection and Characterization of DNA Aptamers for Egg White Lysozyme |
title_fullStr | Selection and Characterization of DNA Aptamers for Egg White Lysozyme |
title_full_unstemmed | Selection and Characterization of DNA Aptamers for Egg White Lysozyme |
title_short | Selection and Characterization of DNA Aptamers for Egg White Lysozyme |
title_sort | selection and characterization of dna aptamers for egg white lysozyme |
topic | aptamer capillary electrophoresis food allergen lysozyme systematic evolution of ligands by exponential enrichment |
url | http://www.mdpi.com/1420-3049/15/3/1127/ |
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