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Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose

Di Lella, S and Ma, L and Díaz Ricci, JC and Rabinovich, GA and Asher, SA and Álvarez, RMS (2009) Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose. Biochemistry, 48 (4). 786 - 791. ISSN 0006-2960

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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. © 2009 American Chemical Society.

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Details

Item Type: Article
Status: Published
Creators/Authors:
CreatorsEmailPitt UsernameORCID
Di Lella, S
Ma, L
Díaz Ricci, JC
Rabinovich, GA
Asher, SAasher@pitt.eduASHER
Álvarez, RMS
Date: 3 February 2009
Date Type: Publication
Journal or Publication Title: Biochemistry
Volume: 48
Number: 4
Page Range: 786 - 791
DOI or Unique Handle: 10.1021/bi801855g
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Refereed: Yes
ISSN: 0006-2960
MeSH Headings: Computer Simulation; Crystallography, X-Ray; Galectin 1--chemistry; Galectin 1--metabolism; Humans; Lactose--chemistry; Lactose--metabolism; Models, Chemical; Protein Binding; Solvents--chemistry; Solvents--metabolism; Spectrum Analysis, Raman; Thermodynamics; Water--chemistry; Water--metabolism
Other ID: NLM NIHMS86763, NLM PMC2633424
PubMed Central ID: PMC2633424
PubMed ID: 19128029
Date Deposited: 08 Feb 2013 20:50
Last Modified: 02 Feb 2019 16:55
URI: http://d-scholarship.pitt.edu/id/eprint/17262

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