ja9b09102_si_001.pdf (2.66 MB)
A Synthetic Vesicle-to-Vesicle Communication System
journal contribution
posted on 2019-10-23, 12:06 authored by Yudi Ding, Nicholas H. Williams, Christopher A. HunterA molecular
signal displayed on the external surface of one population of vesicles
was used to trigger a catalytic process on the inside of a second
population of vesicles. The key recognition event is the transfer
of a protein (NeutrAvidin) bound to vesicles displaying desthiobiotin
to vesicles displaying biotin. The desthiobiotin–protein complex
was used to anchor a synthetic transducer in the outer leaflet of
the vesicles, and when the protein was displaced, the transducer translocated
across the bilayer to expose a catalytic headgroup to the internal
vesicle solution. As a result, an ester substrate encapsulated on
the inside of this second population of vesicles was hydrolyzed to
give a fluorescence output signal. The protein has four binding sites,
which leads to multivalent interactions with membrane-anchored ligands
and very high binding affinities. Thus, biotin, which has a dissociation
constant 3 orders of magnitude higher than desthiobiotin, did not
displace the protein from the membrane-anchored transducer, and membrane-anchored
biotin displayed on the surface of a second population of vesicles
was required to generate an effective input signal.
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binding affinitiesvesicle solution3 ordersinput signalbinding sitesproteinmembrane-anchored biotinester substrate encapsulatedfluorescence output signaldesthiobiotinmembrane-anchored transducerrecognition eventtransducer translocatedmembrane-anchored ligandsSynthetic Vesicle-to-Vesicle Communication System
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