Galectin-1-asialofetuin interaction is inhibited by peptides containing the Tyr-Xxx-Tyr motif acting on the glycoprotein

Edit Wéber, A. Hetényi, Balázs Váczi, Éva Szolnoki, R. Fajka-Boja, Vilmos Tubak, E. Monostori, T. Martinek

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Galectin-1 (Gal-1), a ubiquitous β-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 b-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. 15N,1H HSQC titrations with 15N-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.

Original languageEnglish
Pages (from-to)228-234
Number of pages7
JournalChemBioChem
Volume11
Issue number2
DOIs
Publication statusPublished - Jan 25 2010

Fingerprint

Galectin 1
Glycoproteins
Peptides
Galactosides
Glycoconjugates
Cell proliferation
Sexually Transmitted Diseases
Titration
Sugars
Autoimmune Diseases
asialofetuin
Cell Survival
Carrier Proteins
Cell Proliferation
Nuclear magnetic resonance
Tissue

Keywords

  • Galectins
  • Glycomimetics
  • Lectin mimetics
  • NMR spectroscopy
  • Peptides

ASJC Scopus subject areas

  • Biochemistry
  • Organic Chemistry
  • Molecular Medicine
  • Molecular Biology

Cite this

Galectin-1-asialofetuin interaction is inhibited by peptides containing the Tyr-Xxx-Tyr motif acting on the glycoprotein. / Wéber, Edit; Hetényi, A.; Váczi, Balázs; Szolnoki, Éva; Fajka-Boja, R.; Tubak, Vilmos; Monostori, E.; Martinek, T.

In: ChemBioChem, Vol. 11, No. 2, 25.01.2010, p. 228-234.

Research output: Contribution to journalArticle

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