Abstract:
:Substantial efforts have been made to understand the interactions between immune checkpoint receptors and their ligands targeted in immunotherapies against cancer. To carefully characterize the complete network of interactions involved and the binding affinities between their extracellular domains, an improved kinetic assay is needed to overcome limitations with surface plasmon resonance (SPR). Here, we present a magneto-nanosensor platform integrated with a microfluidic chip that allows measurement of dissociation constants in the micromolar-range. High-density conjugation of magnetic nanoparticles with prey proteins allows multivalent receptor interactions with sensor-immobilized bait proteins, more closely mimicking natural-receptor clustering on cells. The platform has advantages over traditional SPR in terms of insensitivity of signal responses to pH and salinity, less consumption of proteins and better sensitivities. Using this platform, we characterized the binding affinities of the PD-1-PD-L1/PD-L2 co-inhibitory receptor system, and discovered an unexpected interaction between the two known PD-1 ligands, PD-L1 and PD-L2.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Lee JR,Bechstein DJ,Ooi CC,Patel A,Gaster RS,Ng E,Gonzalez LC,Wang SXdoi
10.1038/ncomms12220subject
Has Abstractpub_date
2016-07-22 00:00:00pages
12220issn
2041-1723pii
ncomms12220journal_volume
7pub_type
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