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Dataset of the binding kinetic rate constants of anti-PCSK9 antibodies obtained using the Biacore T100, ProteOn XPR36, Octet RED384, and IBIS MX96 biosensor platforms

Here we provide data from a head-to-head comparison study using four biosensor platforms: GE Healthcare׳s Biacore T100, Bio-Rad׳s ProteOn XPR36, ForteBio׳s Octet RED384, and Wasatch Microfluidics׳s IBIS MX96. We used these instruments to analyze the binding interactions of a panel of ten high-affini...

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Detalles Bibliográficos
Autores principales: Yang, Danlin, Singh, Ajit, Wu, Helen, Kroe-Barrett, Rachel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4979041/
https://www.ncbi.nlm.nih.gov/pubmed/27547794
http://dx.doi.org/10.1016/j.dib.2016.07.044
Descripción
Sumario:Here we provide data from a head-to-head comparison study using four biosensor platforms: GE Healthcare׳s Biacore T100, Bio-Rad׳s ProteOn XPR36, ForteBio׳s Octet RED384, and Wasatch Microfluidics׳s IBIS MX96. We used these instruments to analyze the binding interactions of a panel of ten high-affinity monoclonal antibodies with their antigen, human proprotein convertase subtilisin kexin type 9 (PCSK9). For each instrument, binding curves obtained at multiple densities of surface antibodies were fit to the 1:1 Langmuir kinetic model, and the association and dissociation rate constants and corresponding affinity constants were calculated. The data supplied in this article accompany the research article entitled, “Comparison of biosensor platforms in the evaluation of high affinity antibody–antigen binding kinetics” (Yang et al., 2016) [1], which further discusses the strengths and weaknesses of each biosensor platform with an emphasis on data consistency, comparability, and operational efficiency.