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

Edit Wéber, Anasztázia Hetényi, Balázs Váczi, Éva Szolnoki, Roberta Fajka-Boja, Vilmos Tubak, Éva Monostori, Tamás A. Martinek

Research output: Contribution to journalArticle

6 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

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Organic Chemistry

Fingerprint Dive into the research topics of 'Galectin-1-asialofetuin interaction is inhibited by peptides containing the Tyr-Xxx-Tyr motif acting on the glycoprotein'. Together they form a unique fingerprint.

  • Cite this