Critical Role of the Solvent Environment in Galectin-1 Binding to the Disaccharide Lactose
Open Access
- 7 January 2009
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 48 (4), 786-791
- https://doi.org/10.1021/bi801855g
Abstract
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.This publication has 39 references indexed in Scilit:
- Functions of cell surface galectin-glycoprotein latticesCurrent Opinion in Structural Biology, 2007
- Synthetic lactulose amines: novel class of anticancer agents that induce tumor-cell apoptosis and inhibit galectin-mediated homotypic cell aggregation and endothelial cell morphogenesisGlycobiology, 2005
- The Amber biomolecular simulation programsJournal of Computational Chemistry, 2005
- Growth-regulatory Human Galectin-1: Crystallographic Characterisation of the Structural Changes Induced by Single-site Mutations and their Impact on the Thermodynamics of Ligand BindingJournal of Molecular Biology, 2004
- Raman structural markers of tryptophan and histidine side chains in proteinsPeptide Science, 2003
- UV resonance Raman spectroscopy for analytical, physical, and biophysical chemistry. Part 2Analytical Chemistry, 1993
- Effect of hydrophobic environment on the resonance Raman spectra of tryptophan residues in proteinsJournal of Raman Spectroscopy, 1992
- Origin of the doublet at 1360 and 1340 cm−1 in the Raman spectra of tryptophan and related compoundsSpectrochimica Acta Part A: Molecular Spectroscopy, 1986
- Normal coordinate analysis of the indole ringSpectrochimica Acta Part A: Molecular Spectroscopy, 1986
- UV resonance Raman studies of acetone, acetamide, and N-methylacetamide: models for the peptide bondThe Journal of Physical Chemistry, 1985