Conformational studies on phenyl thioglycosides: a remote effect on disaccharide linkage by phenyl aglycons attenuates recognition of galabiosides by a bacterial adhesin.
Phenyl S-galabiosides display altered conformational properties, as compared to phenyl O-galabiosides, characterised by a remote effect on the galabiose intersaccharidic glycoside bond by the phenyl aglycon, resulting in significantly lowered affinity for the PapG class II adhesin of uropathogenic E. coli.
Ohlsson
Jörgen
J
Bioorganic Chemistry, Lund University, POB 124, SE-221 00 Lund, Sweden.
Sundin
Anders
A
Nilsson
Ulf J
UJ
D018829:Adhesins, Bacterial / Q000737:chemistry*; D001665:Binding Sites; D002236:Carbohydrate Conformation; D002448:Cell Adhesion; D004187:Disaccharides / Q000737:chemistry*; D029968:Escherichia coli Proteins; D006801:Humans; D006841:Hydrocarbons, Aromatic / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008968:Molecular Conformation; D011485:Protein Binding; D013865:Thioglycosides / Q000737:chemistry*
D018829:Adhesins, Bacterial; D004187:Disaccharides; D029968:Escherichia coli Proteins; D006841:Hydrocarbons, Aromatic; D013865:Thioglycosides; C032103:4-O-alpha-D-galactopyranosyl-D-galactose