Please use this identifier to cite or link to this item: https://doi.org/10.1007/978-3-540-92841-6_221
Title: Determination of Affinity Constant from Microfluidic Binding Assay
Authors: Tan, D.
Roy, P. 
Keywords: Equilibrium binding
Equilibrium constant
Mathematical model
Microfluidic
Receptor-ligand
Issue Date: 2009
Source: Tan, D.,Roy, P. (2009). Determination of Affinity Constant from Microfluidic Binding Assay. IFMBE Proceedings 23 : 894-897. ScholarBank@NUS Repository. https://doi.org/10.1007/978-3-540-92841-6_221
Abstract: We present a method of determining the affinity constant of a receptor-ligand pair using equilibrium binding in a microfluidic channel. This technique involves the immobilization of the receptor to the microchannel surface and perfusion of the ligand at a fixed flow rate. The ligand concentration in the eluent is monitored in real time. The break-through time of the ligand is then determined and compared with that of an appropriate, non-binding, reference molecule. The difference in break-through time can then be used in a mathematical model we have developed to determine the affinity constant of the receptor-ligand pair. Using this method, we have determined the equilibrium dissociation constant, KD, of a rat anti-insulin immunoglobulin and a fluorescein-conjugated human insulin. Fluorescein-conjugated aprotinin was used as the non-binding reference molecule. Our experiments yielded a KD value of 0.76 μM for this anti-insulin IgG and insulin-FITC pair. © International Federation of Medical and Biological Engineering 2009.
Source Title: IFMBE Proceedings
URI: http://scholarbank.nus.edu.sg/handle/10635/88240
ISBN: 9783540928409
ISSN: 16800737
DOI: 10.1007/978-3-540-92841-6_221
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