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Galectin-1-Asialofetuin Interaction Is Inhibited by Peptides Containing the Tyr-Xxx-Tyr Motif Acting on the Glycoprotein

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

Chembiochem : a European journal of chemical biology, 2010-01, Vol.11 (2), p.228-234 [Periódico revisado por pares]

Weinheim: Wiley-VCH Verlag

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Título:
Galectin-1-Asialofetuin Interaction Is Inhibited by Peptides Containing the Tyr-Xxx-Tyr Motif Acting on the Glycoprotein
Autor: Wéber, Edit ; Hetényi, Anasztázia ; Váczi, Balázs ; Szolnoki, Éva ; Fajka-Boja, Roberta ; Tubak, Vilmos ; Monostori, Éva ; Martinek, Tamás A
Assuntos: alpha-Fetoproteins - antagonists & inhibitors ; alpha-Fetoproteins - metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Asialoglycoproteins - antagonists & inhibitors ; Asialoglycoproteins - metabolism ; Fetuins ; Galectin 1 - antagonists & inhibitors ; Galectin 1 - genetics ; Galectin 1 - metabolism ; galectins ; glycomimetics ; Glycoproteins - metabolism ; Humans ; Jurkat Cells ; lectin mimetics ; Magnetic Resonance Spectroscopy ; NMR spectroscopy ; peptides ; Peptides - chemical synthesis ; Peptides - chemistry ; Peptides - pharmacology ; Protein Binding ; Recombinant Proteins - antagonists & inhibitors ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Tyrosine - chemistry
É parte de: Chembiochem : a European journal of chemical biology, 2010-01, Vol.11 (2), p.228-234
Notas: http://dx.doi.org/10.1002/cbic.200900502
Hungarian Scientific Research Fund - No. OTKA K 69047; No. PD 75938; No. NKTH-OTKA CK 78188; No. OTKA NF 69316
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Descrição: 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 β-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.
Editor: Weinheim: Wiley-VCH Verlag
Idioma: Inglês

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