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| 3. |
- Larsson, Andreas, et al.
(author)
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Quantitative studies of the binding of the class II PapG adhesin from uropathogenic Escherichia coli to oligosaccharides.
- 2003
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In: Bioorganic & Medicinal Chemistry. - : Elsevier. - 0968-0896 .- 1464-3391. ; 11:10, s. 2255-2261
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Journal article (peer-reviewed)abstract
- Binding of the class II PapG adhesin, found at the tip of filamentous pili on Escherichia coli, to the carbohydrate moiety of globoseries glycolipids in the human kidney is a key step in development of pyelonephritis, a severe form of urinary tract infection. An assay based on surface plasmon resonance for quantification of the binding of the class II PapG adhesin to oligosaccharides has been developed. Using this assay dissociation constants ranging from 80 to 540 M were determined for binding of the PapG adhesin to di-pentasaccharide fragments from the globoseries of glycolipids. A series of galabiose derivatives, modified at the anomeric position, O-2′ or O-3′, was also investigated. The anomeric position appeared to be the most promising for development of improved inhibitors of PapG-mediated adhesion of E. coli. p-Methoxyphenyl galabioside was found to be most potent (Kd=140 M), and binds to PapG almost as well as the Forssman pentasaccharide.
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| 6. |
- Ohlsson, Jörgen, et al.
(author)
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Discovery of potent inhibitors of PapG adhesins from uropathogenic Escherichia coli through synthesis and evaluation of galabiose derivatives
- 2002
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In: ChemBioChem. - 1439-4227. ; 3:8, s. 772-779
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Journal article (peer-reviewed)abstract
- The synthesis of two galabioside (Golalpha1-4Gal) collections based on diversification at the O-1 and O-3' atoms is reported. The galabiosides were evaluated as inhibitors of hemagglutination of human erythrocytes by two strains of Escherichia coli that expressed the class I and class II PapG adhesins, respectively. The class I adhesin. was found to prefer aromatic substituents both at the O-1 and the O-3' position of the galabiose disaccharide. One galabioside, p-methoxyphenyl [3-O-(m-nitrobenzyl)-alpha-D-galacto-pyranosyl]-(1-4)-beta-D-galactopyro noside], had an IC50 value of 4.1 mum, which is the best inhibition of the class I adhesin to date.
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| 7. |
- Andersson, LK, et al.
(author)
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The effect of glycosylation on the structure of designed four-helix bundle motifs
- 2000
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In: JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS 2. - 0300-9580. ; :3, s. 459-464
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Journal article (peer-reviewed)abstract
- A galactose-, 1, and a cellobiose derivative, 2, have been site selectively, post-translationally, incorporated into a folded helix-loop-helix dimer LA-42b in a one step reaction at room temperature. The structural effects on the folded peptide upon glycosylation have been studied by CD and NMR spectroscopy. The negative value of the mean residue ellipticity of the folded peptide, LA-42b, was raised from -19000 +/- 1000 to -21200 +/- 1000 deg cm(2) dmol(-1) upon introduction of the galactose derivative and to -19500 +/- 1000 deg cm(2) dmol(-1) upon introduction of the cellobiose derivative, showing that the helical content was increased. The dissociation constant of the dimer decreased from 120 to 30 mu M upon glycosylation. The introduction of 1 into GTD-C, a folded helix-loop-helix dimer with a well defined tertiary structure, had little structural impact. Glycosylation stabilises the folded structure of proteins with partially exposed hydrophobic cores but has little effect on well-packed proteins.
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| 9. |
- Holm, B, et al.
(author)
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Glycopeptide specificity of helper T cells obtained in mouse models for rheumatoid arthritis
- 2002
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In: ChemBioChem. - 1439-4227. ; 3:12, s. 1209-1222
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Journal article (peer-reviewed)abstract
- Five protected analogues of beta-D-galctosyl-(5R)-5-hydroxy-L-lysine were prepared, in which the galactosyl moiety was modified by monodeoxygenation or inversion of stereochemistry at C-4. The building blocks were used in the solid-phase synthesis of a set of glycopeptides related to the peptide fragment CII256-273 from type II collagen. Evaluation of the glycopeptides revealed that T-cell hybridomas obtained in collagen-induced arthiritis (CIA), which is a common mouse model for rheumatoid arthritis, recognized the galactosyl moiety with high specificity for individual hydroxy groups. Moreover, T-cell hybridomas obtained in a humanized variant of CIA were also found to recognize the glycopeptides in an equally carbohydrate-specific manner. The results allowed the generation of models of the complexes formed between the appropriate class II major histocompatibilty complex (MHC) molecule, glycopeptide, and the T-cell receptor, that is, of an interaction that is critical for the stimulation of T cells in the arthiritis models. In the structural models, peptide side chains anchor the glycopeptide in pockets in the class II MHC molecule, whereas the galactosylated hydroxylisine residue forms the key contacts with the T-cell receptor. Importantly, the results also suggest that a T-cell response towards glycopeptide fragments from type II collagen could play an important role in the development of rheumatoid arthiritis in humans.
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| 10. |
- Kihlberg, Steve, et al.
(author)
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Integrate Ergonomics into Production System Design
- 2001
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In: 16th International Conference on Production Research : ICPR - 16 ; 29 July - 3 August 2001, Prague, Czech Republic, Editors: D. Hanus an Talácko, J.. - 8002014383
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Conference paper (other academic/artistic)
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