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The multivalent inhibition of bacterial lectins
Author
The multivalent inhibition of bacterial lectins
Louis Honselaar
Academy of Technology for Health and Environment
Avans Hogeschool, Breda
Universiteit Utrecht
Abstract
The bacterial binding lectin LecA is a beneficial target to prevent the presence of the bacterium P.aeruginosa to its host.
The study of Ou Fu et al. [1] has shown that divalent ligands with two terminal galactoside variants associated with
alternating glucose- triazole spacers are very effective inhibitors. This molecule also proved to have good solubility in
water and it appeared that three triazole spacers were the optimal length for LecA inhibition. In this study, positively
charged, negatively charged and lipophilic ligands were tested although these are good LecA ligands, no improved binding
to LecA can be seen.In this research a molecule is synthesized that can be synthesized with a tetravalent inhibitor. This
could help with the anti-infection properties of the ligand. Figure 1 shows the tetravalent molecule. The reaction overview
is shown in figure 2. The aim of this research project is to synthesize (7) tetraethylene glycol di (2,5-diiodo-4-
methoxybenzene with (5) 4-methoxyphenol as the starting product. The final product (7) is a precurser for the synthesis
of the The tetravalent multivalent inhibitor (2). The analyzes inhibition used for the of fastening bacterial of products and lectins
the final product are TLC, FTIR and 1H-
NMR, and the conversion at each synthesis step.
Keywords: LecA, P. aeruginosa, divalent ligand, tetravalent ligand
Table of content
Figure 1 : Reaction overview fort he synthesis of
tetraethylene glycol di(2,5-diiodo-4-methoxyphenoll.
Figure 2: LecA inhibitor.
[1] A. V. P. H. C. Q. v. U. J. K. N. J. d. M. R. J. P. Ou Fu, „Functionalization of a Rigid Divalent Ligand for LecA, a Bacterial
Adhesion Lectin,” ChemPubSoc Europe, pp. 463-470, 2015.
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