@article{MTMT:1321061, title = {Galectin-1-Asialofetuin Interaction Is Inhibited by Peptides Containing the Tyr-Xxx-Tyr Motif Acting on the Glycoprotein}, url = {https://m2.mtmt.hu/api/publication/1321061}, author = {Wéber, Edit and Hetényi, Anasztázia and Váczi, Balázs and Szolnoki, Éva Tünde and Fajka-Boja, Roberta and Tubak, Vilmos and Monostori, Éva and Martinek, Tamás}, doi = {10.1002/cbic.200900502}, journal-iso = {CHEMBIOCHEM}, journal = {CHEMBIOCHEM}, volume = {11}, unique-id = {1321061}, issn = {1439-4227}, abstract = {Galectin-1 (Gal-1), a ubiquitous P-galactoside-binding protein expressed by various normal and pathological tissues, has been implicated in cancer and autoimmune/inflammatory diseases in consequence of its regulatory role in adhesion, cell viability, proliferation, and angiogenesis. The functions of Gal-1 depend on its affinity for P-galactoside-containing glycoconjugates; accordingly, the inhibition of sugar binding blocks its functions, hence promising potential therapeutic tools. The Tyr-Xxx-Tyr peptide motifs have been reported to be glycomimetic sequences, mainly on the basis of their inhibitory effect on the Gal-1-asialofetuin (ASF) interaction. However, the results regarding the efficacy of the Tyr-Xxx-Tyr motif as a glycomimetic inhibitor are still controversial. The present STD and trNOE NMR experiments reveal that the Tyr-Xxx-Tyr peptides studied do not bind to Gal-1, whereas their binding to ASF is clearly detected. N-15,H-1 HSQC titrations with N-15-labeled Gal-1 confirm the absence of any peptide-Gal-1 interaction. These data indicate that the Tyr-Xxx-Tyr peptides tested in this work are not glycomimetics as they interact with ASF via an unrevealed molecular linkage.}, keywords = {CROSS-LINKING; LIGAND-BINDING; NMR-SPECTROSCOPY; NMR spectroscopy; galectins; Biochemistry & Molecular Biology; glycomimetics; lectin mimetics; (GLYCO)PEPTIDE LIBRARIES; RECOMBINANT GALECTIN-1; CARBOHYDRATE-BINDING; MAMMALIAN GALECTINS; CYTOKINE SECRETION; CELL APOPTOSIS}, year = {2010}, eissn = {1439-7633}, pages = {228-234}, orcid-numbers = {Wéber, Edit/0000-0002-5904-0619; Hetényi, Anasztázia/0000-0001-8080-6992; Fajka-Boja, Roberta/0000-0001-5331-8280; Tubak, Vilmos/0000-0002-6141-3920; Monostori, Éva/0000-0002-7442-3562; Martinek, Tamás/0000-0003-3168-8066} }