Probing the Force-Induced Dissociation of Aptamer-Protein Complexes
| Autor: | Jeroen Lammertyn, M. Kemper, Dragana Spasic, Leo J. van IJzendoorn, Menno Willem Jose Prins, Elena Pérez-Ruiz, Ann Gils |
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| Přispěvatelé: | Molecular Biosensing for Med. Diagnostics, Departmental Office BMT, ICMS Business Operations |
| Rok vydání: | 2014 |
| Předmět: |
0303 health sciences
Base Sequence Chemistry Dissociation rate Aptamer 010401 analytical chemistry Proteins Nanotechnology Aptamers Nucleotide Surface Plasmon Resonance 01 natural sciences Dissociation (chemistry) 0104 chemical sciences Analytical Chemistry 03 medical and health sciences Chemical physics Intermediate state Base sequence Dissociation kinetics Surface plasmon resonance Protein Binding 030304 developmental biology |
| Zdroj: | Analytical Chemistry, 86(6), 3084-3091. American Chemical Society |
| ISSN: | 1520-6882 0003-2700 |
| Popis: | Aptamers are emerging as powerful synthetic bioreceptors for fundamental research, diagnostics, and therapeutics. For further advances, it is important to gain a better understanding of how aptamers interact with their targets. In this work, we have used magnetic force-induced dissociation experiments to study the dissociation process of two different aptamer-protein complexes, namely for hIgE and Ara h 1. The measurements show that both complexes exhibit dissociation with two distinct regimes: the dissociation rate depends weakly on the applied force at high forces but depends stronger on force at low forces. We attribute these observations to the existence of at least one intermediate state and at least two energy barriers in the aptamer-protein interaction. The measured spontaneous dissociation rate constants were validated with SPR using both Biacore and fiber optic technology. This work demonstrates the potential of the magnetic force-induced dissociation approach for an in-depth study of the dissociation kinetics of aptamer-protein bonds, which is not possible with SPR technologies. The results will help in the development and expansion of aptamers as bioaffinity probes. ispartof: Analytical Chemistry vol:86 issue:6 pages:3084-3091 ispartof: location:United States status: published |
| Databáze: | OpenAIRE |
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