Author: Courtney Mycroft-West; Dunhao Su; Stefano Elli; Scott Guimond; Gavin Miller; Jeremy Turnbull; Edwin Yates; Marco Guerrini; David Fernig; Marcelo Lima; Mark Skidmore
Title: The 2019 coronavirus (SARS-CoV-2) surface protein (Spike) S1 Receptor Binding Domain undergoes conformational change upon heparin binding Document date: 2020_3_2
ID: 0d77ojnb_16
Snippet: When 65 nM SARS-CoV-2 S1 RBD was injected over the three sensing channels, there was an initial decrease in signal, followed by an increase, indicative of binding ( Fig. 1B between red arrows) . The initial decrease was due to a slightly lower refractive index of the SARS-CoV-2 S1 RBD protein solution compared to the PBS of the running buffer, which caused a negative bulk shift. This is demonstrated by the injection of 65 nM solution over the con.....
Document: When 65 nM SARS-CoV-2 S1 RBD was injected over the three sensing channels, there was an initial decrease in signal, followed by an increase, indicative of binding ( Fig. 1B between red arrows) . The initial decrease was due to a slightly lower refractive index of the SARS-CoV-2 S1 RBD protein solution compared to the PBS of the running buffer, which caused a negative bulk shift. This is demonstrated by the injection of 65 nM solution over the control channel, functionalized with just streptavidin, where there was a decrease in response, followed by a return to baseline when the channel was returned to running buffer (Fig. 1C, between red arrows) . These data demonstrate that the SARS-CoV-2 S1 RBD protein binds specifically to heparin immobilised through its reducing-end and fails to bind to the underlying streptavidin / ethyleneglycol surface.
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