Book of abstracts version 5

The inhibition of the Pseudomonas Aeruginosa bacteria
Author
Mariët Bakker
Academy of Technology for Health and Environment
Avans Hogeschool, Breda
Universiteit Utrecht
Nishant Sewgobind
Abstract
The bacterial adhesion lectin LecA is an attractive target for the interference with the infectivity of its producer
Pseudomonas Aeruginosa.[1] Divalent ligands with two terminal galactoside moieties were shown to be potent inhibitors.
In hopes of further enhancing the LecA inhibitory, a divalent galactoside ligand will be expanded to a quadrupole
galactoside ligand, as shown in Figure 1. The linking between two divalent galactosides takes place through a PEG -
coupling molecule (8). [2]
In this research, the starting material for synthesizing the PEG-molecule is 1,4-dimethoxybenzene(2). The synthesis route
is shown in Figure 2. The first step is the halogenation of 1,4 -dimethoxybenzene(2). After the synthesis of 2,5-diiodo-1,4-
dimethoxybenzene(4), the product has reacted with a [TMAH][Al 2Cl 7] complex to replace a methoxide group for a
hydroxyl group. The third step is the synthesis of ditosyl tetraethylenegycol( 7), which can react with the demethylated
phenol(4) to form the PEG coupling molecule called 2,5-diiodo-4-methoxyphenol. The reactions were followed with TLC
and the products were analyzed by FTIR and HNMR.
Keywords: LecA, Pseudomonas Aeruginosa, PEG, halogenation, demethylation
Table of content
Figure 1: Two divalent galactosides are coupled by a PEG. Figure 2: The synthesis routes in this research.
[1] Novoa, Alexandre. Eierhoff, Thorsten. Topin, Jérémie. “A LecA Ligand Identified from a Galactoside-Conjugate Array
Inhibits Host Cell Invasion by Pseudomonas aeruginosa”. Angewandte Chemie. (2014)
[2] Bouvier, Benjamin. “Optimizing the multivalent binding of bacterial Lectin LecA by glycopeptide dendrimers for
therapeutic purposes”. Journal of Chemical information and modelling, ACS publications (2016)
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