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

Publikation: Beitrag in FachzeitschriftForschungsartikelBeigetragenBegutachtung



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.


Seiten (von - bis)27-36
FachzeitschriftBiosensors : open access journal
PublikationsstatusVeröffentlicht - 19 Jan. 2015

Externe IDs

PubMedCentral PMC4384080
Scopus 84925965005