Biosensors | |
Kinetic Analyses of Data from a Human Serum Albumin Assay Using the liSPR System | |
Anja Henseleit3  Carolin Pohl3  Hans-Michael Kaltenbach2  Karina Hettwer2  Kirsten Simon1  Steffen Uhlig2  Natalie Haustein3  Thomas Bley3  Elke Boschke3  | |
[1] New diagnostics GmbH, Moosstraße 92c, Freising D-85356, Germany; E-Mail:;QuoData GmbH, Prellerstraße 14, Dresden 01309, Germany; E-Mails:;Institute of Food Technology and Bioprocess Engineering, Technische Universität Dresden, Dresden 01062, Germany; E-Mails: | |
关键词: surface plasmon resonance (SPR); human serum albumin (HSA); antibody; bivalent analyte; | |
DOI : 10.3390/bios5010027 | |
来源: mdpi | |
【 摘 要 】
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.
【 授权许可】
CC BY
© 2015 by the authors; licensee MDPI, Basel, Switzerland.
【 预 览 】
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