Accounting for unintended binding events in the analysis of quartz crystal microbalance kinetic data

作者：Heller Gabriella T; Zwang Theodore J; Sarapata Elizabeth A; Haber Michael A; Sazinsky Matthew H; Radunskaya Ami E; Johal Malkiat S^*

来源：Colloids and Surfaces B: Biointerfaces , 2014, 117: 425-431.

DOI：10.1016/j.colsurfb.2014.02.044

• QCM-D
• Unintended interactions
• Nonspecific interactions
• Kinetics
• Dissociation constant

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.

• 出版日期2014-5-1