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Biosensors 2015, 5(1), 27-36; doi:10.3390/bios5010027

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

Institute of Food Technology and Bioprocess Engineering, Technische Universität Dresden, Dresden 01062, Germany
QuoData GmbH, Prellerstraße 14, Dresden 01309, Germany
New diagnostics GmbH, Moosstraße 92c, Freising D-85356, Germany
Author to whom correspondence should be addressed.
Academic Editor: Jeff D. Newman
Received: 9 September 2014 / Revised: 26 September 2014 / Accepted: 19 December 2014 / Published: 19 January 2015
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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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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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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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