Abstract
Site specific labeling methods have significant potential to enhance the properties of antibody conjugates. While studied extensively in the context of antibody-drug conjugates (ADCs), few studies have examined the impact of homogenous labeling on the properties of antibody-fluorophore conjugates (AFCs). We report the application of pentafluorophenyl (PFP) esters, which had previously been shown to be reasonably selective for K188 of the kappa light chain of human IgG antibodies, toward producing AFCs. We show that simple replacement of N-hydroxy succinimide (NHS) with PFP dramatically increases the light-chain specificity of near-infrared (NIR) AFCs. Comparing the properties of AFCs labeled using NHS and PFP-activated esters reveals that the latter exhibits reduced aggregation and improved brightness, both in vitro and in vivo. Overall, the use of PFP esters provides a remarkably simple approach to provide selectively labeled antibodies with improved properties.
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