Abstract

Surface plasmon resonance (SPR) is a label-free biophysical technique that is widely used to investigate biomolecular interactions and a very powerful tool useful in different stages of small molecule drug development and antibody characterization. Direct molecular binding on the SPR chip surface is recorded as a response in real time. Several experimental variables, including buffer composition, type of sensor chip, coupling chemistry of molecules on the sensor surface, and surface regeneration conditions, contribute to quality and accuracy of the SPR data.

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