Kinetic Analyses of Data from a Human Serum Albumin Assay Using the liSPR System.
Biosensors (Basel)
; 5(1): 27-36, 2015 Jan 19.
Article
em En
| MEDLINE
| ID: mdl-25607476
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 (11 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 â LA + L â LLA). The apparent binding affinity for this model measured 37 pM for the first reaction step, and 20 pM for the second step.
Texto completo:
1
Base de dados:
MEDLINE
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article