Kinetic Analyses of Data from a Human Serum Albumin Assay Using the liSPR System
Publikation: Beitrag in Fachzeitschrift › Forschungsartikel › Beigetragen › Begutachtung
Beitragende
Abstract
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.
Details
Originalsprache | Englisch |
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Seiten (von - bis) | 27-36 |
Seitenumfang | 10 |
Fachzeitschrift | Biosensors : open access journal |
Jahrgang | 5 |
Ausgabenummer | 1 |
Publikationsstatus | Veröffentlicht - 19 Jan. 2015 |
Peer-Review-Status | Ja |
Externe IDs
PubMedCentral | PMC4384080 |
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Scopus | 84925965005 |