0000000001194878

AUTHOR

Fernanda C. Carvalho

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Evidence for Conformational Mechanism on the Binding of TgMIC4 with β-Galactose-Containing Carbohydrate Ligand

2015

A deeper understanding of the role of sialic/desialylated groups during TgMIC4-glycoproteins interactions has importance to better clarify the odd process of host cell invasion by members of the apicomplexan phylum. Within this context, we evaluated the interaction established by recombinant TgMIC4 (the whole molecule) with sialylated (bovine fetuin) and desialylated (asialofetuin) glycoproteins by using functionalized quartz crystal microbalance with dissipation monitoring (QCM-D). A suitable receptive surface containing recombinant TgMIC4 for monitoring β-galactose-containing carbohydrate ligand (limit of quantification ∼ 40 μM) was designed and used as biomolecular recognition platform t…

Conformational changemedia_common.quotation_subjectCarbohydratesMolecular ConformationProtozoan ProteinsContext (language use)Plasma protein bindingLigandsElectrochemistryGeneral Materials ScienceInternalizationSpectroscopymedia_commonchemistry.chemical_classificationChemistryLigandLECTINASGalactoseSurfaces and InterfacesCondensed Matter PhysicsFetuinBiochemistryQuartz Crystal Microbalance TechniquesAdsorptionTarget proteinGlycoproteinToxoplasmaProtein BindingLangmuir
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