Ding, Yudi Williams, Nicholas H. Hunter, Christopher A. A Synthetic Vesicle-to-Vesicle Communication System A 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. binding affinities;vesicle solution;3 orders;input signal;binding sites;protein;membrane-anchored biotin;ester substrate encapsulated;fluorescence output signal;desthiobiotin;membrane-anchored transducer;recognition event;transducer translocated;membrane-anchored ligands;Synthetic Vesicle-to-Vesicle Communication System 2019-10-23
    https://acs.figshare.com/articles/journal_contribution/A_Synthetic_Vesicle-to-Vesicle_Communication_System/10028621
10.1021/jacs.9b09102.s001