Accounting for unintended binding events in the analysis of quartz crystal microbalance kinetic data.
Autor: | Heller GT; Chemistry Department, Pomona College, 645 North College Avenue, Claremont, CA 91711, United States., Zwang TJ; Chemistry Department, Pomona College, 645 North College Avenue, Claremont, CA 91711, United States., Sarapata EA; Mathematics Department, Pomona College, 610 North College Avenue, Claremont, CA 91711, United States., Haber MA; Chemistry Department, Pomona College, 645 North College Avenue, Claremont, CA 91711, United States., Sazinsky MH; Chemistry Department, Pomona College, 645 North College Avenue, Claremont, CA 91711, United States., Radunskaya AE; Mathematics Department, Pomona College, 610 North College Avenue, Claremont, CA 91711, United States., Johal MS; Chemistry Department, Pomona College, 645 North College Avenue, Claremont, CA 91711, United States. Electronic address: malkiat.johal@pomona.edu. |
---|---|
Jazyk: | angličtina |
Zdroj: | Colloids and surfaces. B, Biointerfaces [Colloids Surf B Biointerfaces] 2014 May 01; Vol. 117, pp. 425-31. Date of Electronic Publication: 2014 Mar 12. |
DOI: | 10.1016/j.colsurfb.2014.02.044 |
Abstrakt: | Previous methods for analyzing protein-ligand binding events using the quartz crystal microbalance with dissipation monitoring (QCM-D) fail to account for unintended binding that inevitably occurs during surface measurements and obscure kinetic information. In this article, we present a system of differential equations that accounts for both reversible and irreversible unintended interactions. This model is tested on three protein-ligand systems, each of which has different features, to establish the feasibility of using the QCM-D for protein binding analysis. Based on this analysis, we were able to obtain kinetic information for the intended interaction that is consistent with those obtained in literature via bulk-phase methods. In the appendix, we include a method for decoupling these from the intended binding events and extracting relevant affinity information. (Copyright © 2014 Elsevier B.V. All rights reserved.) |
Databáze: | MEDLINE |
Externí odkaz: |