Intrinsic tryptophan fluorescence spectroscopy reliably determines galectin-ligand interactions.

ABSTRACT: Galectins are involved in the regulation of divergent physiological and pathological processes and are increasingly recognized to play important roles in a number of diseases. However, a simple and effective way in assessing galectin-ligand interactions is lacking. Our examination of the sequence of all 12 human galectin members reveals the presence of one or more tryptophan residues in the carbohydrate-recognition domains of each galectin. This led us to investigate the possibility that alteration of the galectin intrinsic tryptophan fluorescence could be used in determining the strength of galectin-ligand interactions. One representative member from each of the three subtype galectins, galectin-2 (proto-), galectin-3 (chimera-) and galectin-4 (tandem repeat-type), was selected and analys

SUBMITTER: Sindrewicz P 

PROVIDER: S-EPMC6694196 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature