biostudies-literatureUnknown9(1)Paulikova GA recently described bangle lectin (PHL) from the bacterium Photorhabdus asymbiotica was identified as a mainly fucose-binding protein that could play an important role in the host-pathogen interaction and in the modulation of host immune response. Structural studies showed that PHL is a homo-dimer that contains up to seven L-fucose-specific binding sites per monomer. For these reasons, potential ligands of the PHL lectin: α-L-fucopyranosyl-containing mono-, di-, tetra-, hexa- and dodecavalent ligands were tested. Two types of polyvalent structures were investigated - calix[4]arenes and dendrimers. The shared feature of all these structures was a C-glycosidic bond instead of the more common but physiologically unstable O-glycosidic bond. The inhibition potential of the tested structures waScientific reports14904https://www.ebi.ac.uk/biostudies/studies/S-EPMC6797808biostudies-literatureFucosylated inhibitors of recently identified bangle lectin from Photorhabdus asymbiotica.PMC6797808Wimmerova MParkan KMoravcova JBertolotti BOroszova BPaulikova GHouser JKasakova MfalseFucosylated inhibitors of recently identified bangle lectin from Photorhabdus asymbiotica.A recently described bangle lectin (PHL) from the bacterium Photorhabdus asymbiotica was identified as a mainly fucose-binding protein that could play an important role in the host-pathogen interaction and in the modulation of host immune response. Structural studies showed that PHL is a homo-dimer that contains up to seven L-fucose-specific binding sites per monomer. For these reasons, potential ligands of the PHL lectin: α-L-fucopyranosyl-containing mono-, di-, tetra-, hexa- and dodecavalent ligands were tested. Two types of polyvalent structures were investigated - calix[4]arenes and dendrimers. The shared feature of all these structures was a C-glycosidic bond instead of the more common but physiologically unstable O-glycosidic bond. The inhibition potential of the tested structures wa2019-01-01T00:00:00Z2019 Oct2025-04-22T00:40:49.281Z2019-11-05T08:11:54ZS-EPMC67978083162429610.1038/s41598-019-51357-9