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dc.contributor.authorHarrison, Jennifer A.
dc.contributor.authorKartha, K. P. Ravindranathan
dc.contributor.authorFournier, Eric J. L.
dc.contributor.authorLowary, Todd L.
dc.contributor.authorMalet, Carles
dc.contributor.authorNilsson, Ulf J.
dc.contributor.authorHindsgaul, Ole
dc.contributor.authorSchenkman, Sergio [UNIFESP]
dc.contributor.authorNaismith, James H.
dc.contributor.authorField, Robert A.
dc.identifier.citationOrganic & Biomolecular Chemistry. Cambridge: Royal Soc Chemistry, v. 9, n. 5, p. 1653-1660, 2011.
dc.description.abstractSystematically modified octyl galactosides and octyl N-acetyllactosamines were assessed as inhibitors of, and substrates for, T. cruzi trans-sialidase (TcTS) in the context of exploring its acceptor substrate binding site. These studies show that TcTS, which catalyses the alpha-(2 -> 3)-sialylation of non-reducing terminal beta-galactose residues, is largely intolerant of substitution of the galactose 2 and 4 positions whereas substitution of the galactose 6 position is well tolerated. Further studies show that even the addition of a bulky sugar residue (glucose, galactose) does not impact negatively on TcTS binding and turnover, which highlights the potential of 'internal' 6-substituted galactose residues to serve as TcTS acceptor substrates. Results from screening a 93-membered thiogalactoside library highlight a number of structural features (notably imidazoles and indoles) that are worthy of further investigation in the context of TcTS inhibitor development.en
dc.description.sponsorshipWellcome Trust
dc.publisherRoyal Soc Chemistry
dc.relation.ispartofOrganic & Biomolecular Chemistry
dc.rightsAcesso aberto
dc.titleProbing the acceptor substrate binding site of Trypanosoma cruzi trans-sialidase with systematically modified substrates and glycoside librariesen
dc.contributor.institutionJohn Innes Ctr
dc.contributor.institutionUniv St Andrews
dc.contributor.institutionNatl Inst Pharmaceut Educ & Res
dc.contributor.institutionUniv Alberta
dc.contributor.institutionLund Univ
dc.contributor.institutionCarlsberg Lab
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.description.affiliationJohn Innes Ctr, Dept Biol Chem, Norwich NR4 7TJ, Norfolk, England
dc.description.affiliationUniv St Andrews, Ctr Biomol Sci, St Andrews KY16 9ST, Fife, Scotland
dc.description.affiliationNatl Inst Pharmaceut Educ & Res, Dept Med Chem, Sas Nagar 160062, Punjab, India
dc.description.affiliationUniv Alberta, Dept Chem, Edmonton, AB T6G 2G2, Canada
dc.description.affiliationLund Univ, Dept Organ Chem, SE-22100 Lund, Sweden
dc.description.affiliationCarlsberg Lab, DK-2500 Valby, Denmark
dc.description.affiliationUniversidade Federal de São Paulo, Dept Microbiol Immunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Microbiol Immunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.description.sponsorshipIDWellcome Trust: 042472
dc.description.sponsorshipIDWellcome Trust: 040331
dc.description.sourceWeb of Science
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