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Galectin–Glycan Interactions: Guidelines for Monitoring by 77 Se NMR Spectroscopy, and Solvent (H 2 O/D 2 O) Impact on Binding
Author(s) -
Diercks Tammo,
Medrano Francisco J.,
FitzGerald Forrest G.,
Beckwith Donella,
Pedersen Martin Jaeger,
Reihill Mark,
Ludwig AnnaKristin,
Romero Antonio,
Oscarson Stefan,
Cudic Maré,
Gabius HansJoachim
Publication year - 2021
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.202003143
Subject(s) - isothermal titration calorimetry , galectin , heteronuclear molecule , chemistry , nuclear magnetic resonance spectroscopy , circular dichroism , glycan , solvent , stereochemistry , glycoprotein , biochemistry
Functional pairing between cellular glycoconjugates and tissue lectins like galectins has wide (patho)physiological significance. Their study is facilitated by nonhydrolysable derivatives of the natural O‐glycans, such as S‐ and Se‐glycosides. The latter enable extensive analyses by specific 77 Se NMR spectroscopy, but still remain underexplored. By using the example of selenodigalactoside (SeDG) and the human galectin‐1 and ‐3, we have evaluated diverse 77 Se NMR detection methods and propose selective 1 H, 77 Se heteronuclear Hartmann–Hahn transfer for efficient use in competitive NMR screening against a selenoglycoside spy ligand. By fluorescence anisotropy, circular dichroism, and isothermal titration calorimetry (ITC), we show that the affinity and thermodynamics of SeDG binding by galectins are similar to thiodigalactoside (TDG) and N ‐acetyllactosamine (LacNAc), confirming that Se substitution has no major impact. ITC data in D 2 O versus H 2 O are similar for TDG and LacNAc binding by both galectins, but a solvent effect, indicating solvent rearrangement at the binding site, is hinted at for SeDG and clearly observed for LacNAc dimers with extended chain length.