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Monodisperse Sequence‐Controlled α‐ l ‐Fucosylated Glycooligomers and Their Multivalent Inhibitory Effects on LecB
Author(s) -
Bücher Katharina Susanne,
Babic Nikolina,
Freichel Tanja,
Kovacic Filip,
Hartmann Laura
Publication year - 2018
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.201800337
Subject(s) - chemistry , surface plasmon resonance , fucose , biofilm , lectin , biochemistry , ligand (biochemistry) , glycoprotein , bacteria , nanotechnology , biology , receptor , materials science , nanoparticle , genetics
The opportunistic bacterium Pseudomonas aeruginosa , often exhibiting multiresistance against conventional antibiotics, expresses the lectin LecB that is suspected to be an important factor during biofilm formation via interactions with cell‐surface presented carbohydrate ligands such as the blood group antigens. Therefore, carbohydrate‐based ligands interfering with LecB binding have the potential to lead to new anti‐biofilm and anti‐adhesion therapies. This study explores in vitro binding potencies of glycomimetic ligands containing up to six α‐ l ‐fucose ligands on a monodisperse, sequence‐controlled oligoamide scaffold interacting with LecB. Surface plasmon resonance (SPR) and a modified enzyme‐linked lectin assay (mELLA) revealed an increasing affinity to LecB with increasing fucose valency. Furthermore, fucosylated glycooligomers were shown to inhibit the formation of P. aeruginosa biofilm up to 20%. Overall these results show the potential of fucosylated oligoamides to be further developed as inhibitors of LecB binding and biofilm formation.