Advanced high-affinity glycoconjugate ligands of galectins
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
36446202
DOI
10.1016/j.bioorg.2022.106279
PII: S0045-2068(22)00685-X
Knihovny.cz E-zdroje
- Klíčová slova
- Biolayer interferometry, Carbohydrate, Click chemistry, Galectin, Glycoconjugate, Multivalency, Transglycosylation,
- MeSH
- galektiny * metabolismus MeSH
- glykokonjugáty * farmakologie chemie MeSH
- lidé MeSH
- ligandy MeSH
- polysacharidy metabolismus MeSH
- sacharidy chemie MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- galektiny * MeSH
- glykokonjugáty * MeSH
- ligandy MeSH
- polysacharidy MeSH
- sacharidy MeSH
Galectins are proteins of the family of human lectins. By binding terminal galactose units of cell surface glycans, they moderate biological and pathological processes such as cell signaling, cell adhesion, apoptosis, fibrosis, carcinogenesis, and metabolic disorders. The binding of monovalent glycans to galectins is usually relatively weak. Therefore, the presentation of carbohydrate ligands on multivalent scaffolds can efficiently increase and/or discriminate the affinity of the glycoconjugate to different galectins. A library of glycoclusters and glycodendrimers with various structural presentations of the common functionalized N-acetyllactosamine ligand was prepared to evaluate how the mode of presentation affects the affinity and selectivity to the two most abundant galectins, galectin-1 (Gal-1) and galectin-3 (Gal-3). In addition, the effect of a one- to two-unit carbohydrate spacer on the affinity of the glycoconjugates was determined. A new design of the biolayer interferometry (BLI) method with specific AVI-tagged constructs was used to determine the affinity to galectins, and compared with the gold-standard method of isothermal titration calorimetry (ITC). This study reveals new routes to low nanomolar glycoconjugate inhibitors of galectins of interest for biomedical research.
Citace poskytuje Crossref.org
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