Polyvalent Glycan Quantum Dots as a Multifunctional Tool for Revealing Thermodynamic, Kinetic, and Structural Details of Multivalent Lectin–Glycan Interactions
James Hooper, Yuanyuan Liu, Darshita Budhadev, Dario Luis Fernandez Ainaga, Nicole Hondow, Dejian Zhou, Yuan Guo
Abstract
rate, whereas DC-SIGNR gives a rapid initial binding followed by a much slower secondary interaction. We further identify a structural element in DC-SIGN, absent in DC-SIGNR, that plays an important role in maintaining DC-SIGN's MLGI character. Its removal switches the binding from being enthalpically to entropically driven and gives mixed binding modes containing both simultaneous and cross-linking binding behavior, without markedly affecting the overall binding affinity and kinetics.
Topics & Concepts
GlycanDC-SIGNBinding affinitiesReceptor–ligand kineticsAffinitiesPlasma protein bindingLectinBinding siteBiophysicsEnthalpyQuantum dotChemistryNanotechnologyMaterials scienceBiologyBiochemistryGlycoproteinThermodynamicsPhysicsGeneticsAntigenDendritic cellReceptorGlycosylation and Glycoproteins ResearchEscherichia coli research studiesMonoclonal and Polyclonal Antibodies Research