Aubin-Tam, Marie-Eve and Appleyard, David C. and Ferrari, Enrico and Garbin, Valeria and Fadiran, Oluwatimilehin O. and Kunkel, Jacquelyn and Lang, Matthew J. (2011) Adhesion through single peptide aptamers. The Journal of Physical Chemistry A, 115 (16). pp. 3657-3664. ISSN 1089-5639
Full text not available from this repository.Abstract
Aptamer and antibody mediated adhesion is central to biological function and is valuable in the engineering of “lab on a chip” devices. Single molecule force spectroscopy using optical tweezers enables direct nonequilibrium measurement of these noncovalent interactions for three peptide aptamers selected for glass, polystyrene, and carbon nanotubes. A comprehensive examination of the strong attachment between antifluorescein 4−4−20 and fluorescein was also carried out using the same assay. Bond lifetime, barrier width, and free energy of activation are extracted from unbinding histogram data using three single molecule pulling models. The evaluated aptamers appear to adhere stronger than the fluorescein antibody under no- and low-load conditions, yet weaker than antibodies at loads above 25 pN. Comparison to force spectroscopy data of other biological linkages shows the diversity of load dependent binding and provides insight into linkages used in biological processes and those designed for engineered systems.
| Item Type: | Article |
|---|---|
| Additional Information: | Aptamer and antibody mediated adhesion is central to biological function and is valuable in the engineering of “lab on a chip” devices. Single molecule force spectroscopy using optical tweezers enables direct nonequilibrium measurement of these noncovalent interactions for three peptide aptamers selected for glass, polystyrene, and carbon nanotubes. A comprehensive examination of the strong attachment between antifluorescein 4−4−20 and fluorescein was also carried out using the same assay. Bond lifetime, barrier width, and free energy of activation are extracted from unbinding histogram data using three single molecule pulling models. The evaluated aptamers appear to adhere stronger than the fluorescein antibody under no- and low-load conditions, yet weaker than antibodies at loads above 25 pN. Comparison to force spectroscopy data of other biological linkages shows the diversity of load dependent binding and provides insight into linkages used in biological processes and those designed for engineered systems. |
| Keywords: | Aptamers, Force spectroscopy, Single molecule |
| Subjects: | F Physical Sciences > F165 Biomolecular Chemistry C Biological Sciences > C770 Biophysical Science |
| Divisions: | College of Sciences > Faculty of Science > School of Life Sciences |
| Depositing User: | Enrico Ferrari |
| Date Deposited: | 15 Oct 2012 20:21 |
| Last Modified: | 26 Nov 2012 22:43 |
| URI: | http://eprints.lincoln.ac.uk/id/eprint/6579 |
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