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001-es BibID:BIBFORM070763
Első szerző:Kaltner, Herbert
Cím:Bivalent O-glycoside mimetics with S/disulfide/Se substitutions and aromatic core: Synthesis, molecular modeling and inhibitory activity on biomedically relevant lectins in assays of increasing physiological relevance / Herbert Kaltner, Tamás Szabó, Krisztina Fehér, Sabine André, Sára Balla, Joachim C. Manning, László Szilágyi, Hans-Joachim Gabius
Dátum:2017
ISSN:0968-0896
Megjegyzések:The emerging significance of recognition of cellular glycans by lectins for diverse aspects of pathophysiology is a strong incentive for considering development of bioactive and non-hydrolyzable glycoside derivatives, for example by introducing S/Se atoms and the disulfide group instead of oxygen into the glycosidic linkage. We report the synthesis of 12 bivalent thio-, disulfido- and selenoglycosides attached to benzene/naphthalene cores. They present galactose, for blocking a plant toxin, or lactose, the canonical ligand of adhesion/growth-regulatory galectins. Modeling reveals unrestrained flexibility and inter-headgroup distances too small to bridge two sites in the same lectin. Inhibitory activity was first detected by solid-phase assays using a surface-presented glycoprotein, with relative activity enhancements per sugar unit relative to free cognate sugar up to nearly 10fold. Inhibitory activity was also seen on lectin binding to surfaces of human carcinoma cells. In order to proceed to characterize this capacity in the tissue context monitoring of lectin binding in the presence of inhibitors was extended to sections of three types of murine organs as models. This procedure proved to be well-suited to determine relative activity levels of the glycocompounds to block binding of the toxin and different human galectins to natural glycoconjugates at different sites in sections. The results on most effective inhibition by two naphthalene-based disulfides and a selenide raise the perspective for broad applicability of the histochemical assay in testing glycoclusters that target biomedically relevant lectins.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Agglutinin
Glycosyldisulfides
Histochemistry
Lectin
Selenoglycosides
Sugar code
Thioglycosides
Megjelenés:Bioorganic & Medicinal Chemistry. - 25 : 12 (2017), p. 3158-3170. -
További szerzők:Szabó Tamás (1985-) (vegyész) Fehér Krisztina (1974-) (vegyész) André, Sabine Balla Sára Manning, Joachim C. Szilágyi László (1941-) (vegyész) Gabius, Hans-Joachim
Pályázati támogatás:NN-109671
OTKA
GINOP-2.3.2-15-2016-00008
GINOP
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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2.

001-es BibID:BIBFORM099969
035-os BibID:(cikkazonosító)201 (scopus)85122987285 (wos)000746040300001
Első szerző:Timári István (vegyész)
Cím:77Se-Enriched Selenoglycoside Enables Significant Enhancement in NMR Spectroscopic Monitoring of Glycan?Protein Interactions / Timári István, Balla Sára, Fehér Krisztina, Kövér Katalin E., Szilágyi László
Dátum:2022
ISSN:1999-4923
Megjegyzések:Detailed investigation of ligand?protein interactions is essential for better understanding of biological processes at the molecular level. Among these binding interactions, the recognition of glycans by lectins is of particular importance in several diseases, such as cancer; therefore, inhibition of glycan-lectin/galectin interactions represents a promising perspective towards developing therapeutics controlling cancer development. The recent introduction of 77Se NMR spectroscopy for monitoring the binding of a selenoglycoside to galectins prompted interest to optimize the sensitivity by increasing the 77Se content from the natural 7.63% abundance to 99%. Here, we report a convenient synthesis of 77Se-enriched selenodigalactoside (SeDG), which is a potent ligand of the medically relevant human galectin-3 protein, and proof of the expected sensitivity gain in 2D 1H, 77Se correlation NMR experiments. Our work opens perspectives for adding isotopically enriched selenoglycans for rapid monitoring of lectin-binding of selenated as well as non-selenated ligands and for ligand screening in competition experiments.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
77Se isotope
chemical synthesis
glycan
HSQMBC
lectin
ligand?protein binding
NMR spectroscopy
selenodigalactoside
TDG
Megjelenés:Pharmaceutics. - 14 : 1 (2022), p. 1-8. -
További szerzők:Balla Sára Fehér Krisztina (1974-) (vegyész) Kövér Katalin, E. (1956-) (vegyész) Szilágyi László (1941-) (vegyész)
Pályázati támogatás:NN 128368
OTKA
PD 135034
OTKA
GINOP-2.3.3-15-2016-00004
GINOP
GINOP-2.3.2-15-2016-00008
GINOP
ÚNKP-21-5-DE-471
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:
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