Mathematica programming system. This tool can be applied to fit the binding time courses data from multiple label-free platforms and estimate association and dissociation rate constants (k a and k d respectively) for determining apparent dissociation constant (K D) values. The fitting process is automatic, high-throughput and requires minimal knowledge on Mathematica scripting. We demonstrate that the TitrationAnalysis is optimal to analyze antibody-antigen binding data acquired on Biacore T200, Carterra LSA and ForteBio Octet Red384 platforms. The k a , k d and K D values derived using TitrationAnalysis very closely matched the results from the commercial analysis software provided specifically for these instruments. Our analysis tool offers investigators an additional arsenal to analyze binding kinetics data from multiple platforms in a high throughput fashion. Additionally, we have built user directed customizable results output with the appropriate format for perusal in downstream Data Quality Control associated with Good Clinical Laboratory Practice operations. The versatility of TitrationAnalysis to analyze binding kinetics data with high throughput capability and derive k a , k d and K D values closely matching that of native analysis packages from SPR, SPR imaging and BLI platforms offers investigators a powerful alternative in biomolecular interaction analysis.

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