Lectin–glycan interactions are at the heart of
a multitude
of biological events. Glycans are usually presented in a multivalent
manner on the cell surface as part of the so-called glycocalyx, where
they interact with other entities. This multivalent presentation allows
us to overcome the typical low affinities found for individual glycan–lectin
interactions. Indeed, the presentation of glycans may drastically
impact their binding by lectins, highly affecting the corresponding
binding affinity and even selectivity. In this context, we herein
present the study of the interaction of a variety of homo- and heteromultivalent
lactose-functionalized glycomacromolecules and their lipid conjugates
with two human galectins. We have employed as ligands the glycomacromolecules,
as well as liposomes decorated with those structures, to evaluate
their interactions in a cell-mimicking environment. Key details of
the interaction have been unravelled by NMR experiments, both from
the ligand and receptor perspectives, complemented by cryo-electron
microscopy methods and molecular dynamics simulations.
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