Tailor-made Janus lectin with dual avidity assembles glycoconjugate multilayers and crosslinks protocellsElectronic supplementary information (ESI) available: Synthesis procedures of glycopeptides. Sequences of Janus lectins. SDS gels. ESI mass spectra. SPR sensorgrams. QCM-D profile and data molecular models. Control for vesicules binding. See DOI: 10.1039/c8sc02730g

We engineered the first chimeric, bispecific lectin, with two rationally oriented and distinct recognition surfaces. This lectin, coined Janus lectin in allusion to the two-faced roman god, is able to bind independently to both fucosylated and sialylated glycoconjugates. The multivalent presentation...

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Main Authors: Ribeiro, João P, Villringer, Sarah, Goyard, David, Coche-Guerente, Liliane, Höferlin, Manuela, Renaudet, Olivier, Römer, Winfried, Imberty, Anne
Format: Article
Language:English
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Summary:We engineered the first chimeric, bispecific lectin, with two rationally oriented and distinct recognition surfaces. This lectin, coined Janus lectin in allusion to the two-faced roman god, is able to bind independently to both fucosylated and sialylated glycoconjugates. The multivalent presentation of binding sites on each face of the Janus lectin is very efficient, resulting in avidities in the low nanomolar range for both fucosylated and sialylated surfaces. Moreover, novel heterovalent, bifunctional glycoclusters were synthetized that match the topology of the Janus lectin. Based on these tools, we constructed organized and controlled supramolecular architectures by assembling Janus lectin and glycocompound layer-by-layer. Furthermore, the Janus lectin was employed as biomolecular linker to organize protocells made from giant unilamellar vesicles of different nature, to more complex prototissues. In summary, tailor-made Janus lectins open wide possibilities for creating biomimetic matrices or artificial tissues. The double-faced Janus lectin, designed by assembling sialic acid and fucose-specific lectin, organize multivalent heteroglyco compounds in mulitlayered material, and glycosylated protocells in prototissues.
ISSN:2041-6520
2041-6539
DOI:10.1039/c8sc02730g