Conformational Selection in Glycomimetics: Human Galectin-1 Only Recognizes syn-Ψ-Type Conformations of β-1,3-Linked Lactose and Its C-Glycosyl Derivative

• Published in: Chemistry : a European journal Vol. 19; no. 43; pp. 14581 - 14590
• Main Authors: Vidal, Paloma, Roldós, Virginia, Fernández-Alonso, María del Carmen, Vauzeilles, Boris, Bleriot, Yves, Cañada, F. Javier, André, Sabine, Gabius, Hans-Joachim, Jiménez-Barbero, Jesús, Espinosa, Juan Félix, Martín-Santamaría, Sonsoles
• Format: Journal Article
• Language: English
• Published: Weinheim WILEY-VCH Verlag 18.10.2013; WILEY‐VCH Verlag; Wiley-VCH Verlag
• Subjects: Catalysis; Chemical Sciences; conformation analysis; Galectin 1 - chemistry; Galectin 1 - metabolism; glycoconjugates; Glycomics; Glycosides - chemistry; Humans; Hydrogen Bonding; Lactose - chemistry; Molecular Conformation; Molecular Dynamics Simulation; molecular modeling; NMR spectroscopy; Organic chemistry; Other; structure-activity relationships; Substrate Specificity; conformation analysis; structure-activity relationships; NMR spectroscopy; molecular modeling; glycoconjugates

The human lectin galectin‐1 (hGal‐1) translates sugar signals, that is, β‐galactosides, into effects on the level of cells, for example, growth regulation, and has become a model for studying binding of biopharmaceutically relevant derivatives. Bound‐state conformations of Galβ‐C‐(1→3)‐Glcβ‐OMe (1)...