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Open AccessArticle

Kinetic Analyses of Data from a Human Serum Albumin Assay Using the liSPR System

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Institute of Food Technology and Bioprocess Engineering, Technische Universität Dresden, Dresden 01062, Germany
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QuoData GmbH, Prellerstraße 14, Dresden 01309, Germany
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New diagnostics GmbH, Moosstraße 92c, Freising D-85356, Germany
*
Author to whom correspondence should be addressed.
Academic Editor: Jeff D. Newman
Biosensors 2015, 5(1), 27-36; https://doi.org/10.3390/bios5010027
Received: 9 September 2014 / Revised: 26 September 2014 / Accepted: 19 December 2014 / Published: 19 January 2015
We used the interaction between human serum albumin (HSA) and a high-affinity antibody to evaluate binding affinity measurements by the bench-top liSPR system (capitalis technology GmbH). HSA was immobilized directly onto a carboxylated sensor layer, and the mechanism of interaction between the antibody and HSA was investigated. The bivalence and heterogeneity of the antibody caused a complex binding mechanism. Three different interaction models (1:1 binding, heterogeneous analyte, bivalent analyte) were compared, and the bivalent analyte model best fit the curves obtained from the assay. This model describes the interaction of a bivalent analyte with one or two ligands (A + L ↔ LA + L ↔ LLA). The apparent binding affinity for this model measured 37 pM for the first reaction step, and 20 pM for the second step. View Full-Text
Keywords: surface plasmon resonance (SPR); human serum albumin (HSA); antibody; bivalent analyte surface plasmon resonance (SPR); human serum albumin (HSA); antibody; bivalent analyte
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Henseleit, A.; Pohl, C.; Kaltenbach, H.-M.; Hettwer, K.; Simon, K.; Uhlig, S.; Haustein, N.; Bley, T.; Boschke, E. Kinetic Analyses of Data from a Human Serum Albumin Assay Using the liSPR System. Biosensors 2015, 5, 27-36.

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