Multivalent presentation and recognition of complex carbohydrate structures are important in the adhesion processes of pathogens like viruses and bacteria. In spite of the fast evolution of many pathogens, the attachment to specific glycans on cell membranes seems to occur often by multiple conserved binding sites. It has been shown that terminal α-L-fucose is an important attachment factor. Nevertheless, the underlying multivalent binding mechanisms of carbohydrate-mediated adhesion processes are still not well understood and novel model compounds are required to gain new insights.<br/>Monodisperse glyco(oligoamidoamine)s have been shown to be a suitable tool to study multivalent interactions between glycans and lectins of plants and bacteria. Here we show the adaption of the previously presented solid phase polymer synthesis to give a series of monodisperse glycooligomers presenting α-L-fucose units. By the step wise assembly of tailor made building blocks according to previously reported protocols and conjugation of fucose side chains on solid support, the sequence-controlled and multivalent presentation of fucose was realized. Furthermore, variation of number and spacing of fucose units on the oligomeric backbone was achieved. The obtained glycooligomers were then tested for their binding to the capsid protein LecB from pseudomonas aeruginosa, suspected of being responsible for bacterial antibiotic multiresistance. The binding behavior was analyzed using surface plasmon resonance and showed the influence of the different structural parameters onto the binding affinity.

Monodisperse fucosylated glycooligomers to investigate multivalent binding to LecB

255th National Meeting (2018)

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