INQUIMAE   12526
INSTITUTO DE QUIMICA, FISICA DE LOS MATERIALES, MEDIOAMBIENTE Y ENERGIA
Unidad Ejecutora - UE
artículos
Título:
Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose
Autor/es:
DI LELLA, SANTIAGO; MA, LU; DÍAZ RICCI, JUAN CARLOS; RABINOVICH, GABRIEL ADRIÁN; ASHER, SANFORD A.; ÁLVAREZ, ROSA MARÍA SUSANA
Revista:
BIOCHEMISTRY
Editorial:
American Chemical Society
Referencias:
Lugar: Washington, D. C.; Año: 2009 vol. 48 p. 786 - 786
ISSN:
0006-2960
Resumen:
Galectin-1 (Gal-1), a member of a family of evolutionarily conserved glycan-binding proteins, binds specifically to poly-N-acetyllactosamine-enriched glycoconjugates. Through interactions with these glycoconjugates, this protein modulates inflammatory responses and contributes to tumor progression and immune cell homeostasis. The carbohydrate recognition domain includes the single protein tryptophan (Trp68). UV resonance Raman spectroscopy and molecular dynamic simulation were used to examine the change in the environment of the Trp on ligand binding. The UV Raman spectra and the calculated water radial distribution functions show that, while no large structural changes in the protein follow lactose binding, substantial solvent reorganization occurs. These new insights into the microscopic role of water molecules in Gal-1 binding to its specific carbohydrate ligands provides a better understanding of the physicochemical properties of Gal-1-saccharide interactions, which will be useful for the design of synthetic inhibitors for therapeutic purposes.