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Magneto-nanosensor platform for probing low-affinity protein-protein interactions and identification of a low-affinity PD-L1/PD-L2 interaction

Title
Magneto-nanosensor platform for probing low-affinity protein-protein interactions and identification of a low-affinity PD-L1/PD-L2 interaction
Authors
Lee, Jung-RokBechstein, Daniel J. B.Ooi, Chin ChunPatel, AshkaGaster, Richard S.Ng, ElaineGonzalez, Lino C.Wang, Shan X.
Ewha Authors
이정록
Issue Date
2016
Journal Title
Nature Communications
ISSN
2041-1723JCR Link
Citation
Nature Communications vol. 7
Publisher
NATURE PUBLISHING GROUP
Indexed
SCI; SCIE; SCOPUS WOS
Document Type
Article
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.
DOI
10.1038/ncomms12220
Appears in Collections:
엘텍공과대학 > 휴먼기계바이오공학부 > Journal papers
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