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 - 791
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.