Thermodynamic parameters of binding of mouse 2G3 antitheophylline monoclonal antibodies to theophylline

Pokid'ko, Yu. N.; Василов, Р. Г.

doi:10.1007/bf02445681

Cited by 1 publication

(1 citation statement)

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“…The thermodynamic parameters of mouse anti-theophylline monoclonal antibody binding were studied using isothermal titration microcalorimetry. [23] All drug-bovine serum albumin conjugates were commercially available for immobilization on epoxy-coated glass slides. The anti-drug antibodies mixed with human serum at different dilutions reacted with the drug microarray to acquire the binding curves.…”

Section: Introductionmentioning

confidence: 99%

Determination of Bovine Serum Albumin Conjugated Drugs by Immobilization as Microarrays and Oblique-Incidence Reflectivity Difference Microscopy

Sun

Lam

Zhu

2014

Instrumentation Science & Technology

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& Human serum is a mixture of various proteins which may interact with drugs. Therefore, it is of interest to investigate the binding kinetics of pharmaceuticals with their corresponding antibodies in serum. In this article, microarrays and a label-free biosensor were used to study these interactions. Microarrays provide a high-throughput platform for characterizing biomolecular interactions, and the label-free oblique-incidence reflectivity difference biosensor avoids the drawbacks of fluorescencebased methods. The experimental results show that the binding affinities between most of the drugs and their antibodies were reduced in human serum because the bulky proteins block the access to or reduce the stability of the reaction complexes. Therefore, one should be mindful when in vitro or in vivo testing the efficiency of potential drugs and their antibodies.

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Section: Introductionmentioning

confidence: 99%