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Cover Picture: Mannosylated G(0) Dendrimers with Nanomolar Affinities to Escherichia coli FimH (ChemMedChem 8/2007)
Author(s) -
Touaibia Mohamed,
Wellens Adinda,
Shiao Tze Chieh,
Wang Qingan,
Sirois Suzanne,
Bouckaert Julie,
Roy René
Publication year - 2007
Publication title -
chemmedchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.200790025
Subject(s) - surface plasmon resonance , adhesion , chemistry , escherichia coli , dendrimer , pilus , bacterial adhesin , affinities , sonogashira coupling , ligand (biochemistry) , biophysics , microbiology and biotechnology , stereochemistry , nanotechnology , biochemistry , biology , materials science , nanoparticle , receptor , organic chemistry , palladium , gene , catalysis
The cover picture shows fimbriated E. coli (background) expressing mannoside binding pili lectin (FimH) (Connolly surface insert with nanomolar tetrameric mannoside ligand). The FimH are primarily involved in bacterial adhesion to host tissues. The affinity constants of several glycodendrimers were evaluated with surface plasmon resonance (SPR). The understanding of these adhesion phenomena at the molecular level is crucial and presents promising alternatives to traditional antibiotic therapies. A novel class of mannoside clusters (bottom left) was developed using Sonogashira coupling and click chemistry. These mannoside clusters have the potential to inhibit the initial recognition events that lead to adhesion and colonization of host tissues by multiple attachments to E. coli FimH. For details, see the Full Paper by J. Bouckaert, R. Roy, et al. on p. 1190 ff.