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• W2123015220 abstract "Fluorescence-based endpoint detection of microarrays with 10,000 or more molecular targets is a most useful tool for high-throughput profiling of biomolecular interactions, including screening large molecular libraries for novel protein ligands. However, endpoint fluorescence data such as images of reacted microarrays contain little information on kinetic rate constants, and the reliability of endpoint data as measures of binding affinity depends on reaction conditions and postreaction processing. We here report a simultaneous measurement of binding curves of a protein probe with 10,000 molecular targets in a microarray with an ellipsometry-based (label-free) optical scanner. The reaction rate constants extracted from these curves (k(on), k(off), and k(a)=k(on)/k(off)) are used to characterize the probe-target interactions instead of the endpoints. This work advances the microarray technology to a new milestone, namely, from an endpoint assay to a kinetic constant assay platform. The throughput of this binding curve assay platform is comparable to those at the National Institutes of Health Molecular Library Screening Centers, making it a practical method in screening compound libraries for novel ligands and for system-wide affinity profiling of proteins, viruses, or whole cells against diverse molecular targets." @default.
• W2123015220 created "2016-06-24" @default.
• W2123015220 creator A5036818972 @default.
• W2123015220 creator A5044855414 @default.
• W2123015220 creator A5062112272 @default.
• W2123015220 date "2012-06-01" @default.
• W2123015220 modified "2023-09-30" @default.
• W2123015220 title "Simultaneous Measurement of 10,000 Protein-Ligand Affinity Constants Using Microarray-Based Kinetic Constant Assays" @default.
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• W2123015220 doi "https://doi.org/10.1089/adt.2011.0406" @default.
• W2123015220 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3374384" @default.
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