HAL will be down for maintenance from Friday, June 10 at 4pm through Monday, June 13 at 9am. More information
Skip to Main content Skip to Navigation
Journal articles

Engineering the ligand specificity of the human galectin-1 by incorporation of tryptophan analogs

Abstract : Galectin-1 is a β-galactoside-binding lectin with manifold biological functions. A single tryptophan residue (W68) in its carbohydrate binding site plays a major role in ligand binding and is highly conserved among galectins. To fine tune galectin-1 specificity, we introduced several non-canonical tryptophan analogs at this position of human galectin-1 and analyzed the resulting variants using glycan microarrays. Two variants containing 7-azatryptophan and 7fluorotryptophan showed a reduced affinity for 3'-sulfated oligosaccharides. Their interaction with different ligands was further analyzed by fluorescence polarization competition assay. Using molecular modeling we provide structural clues that the change in affinities comes from modulated interactions and solvation patterns. Thus, we show that the introduction of subtle atomic mutations in the ligand binding site of galectin-1 is an attractive approach for finetuning its interactions with different ligands.
Complete list of metadata

https://hal.archives-ouvertes.fr/hal-03517502
Contributor : Anne Imberty Connect in order to contact the contributor
Submitted on : Friday, January 7, 2022 - 6:32:40 PM
Last modification on : Friday, January 21, 2022 - 4:14:01 AM

File

Hal_galectin.pdf
Files produced by the author(s)

Identifiers

Collections

Citation

Felix Tobola, Martin Lepšík, Syeda Rehana Zia, Hakon Leffler, Ulf Nilsson, et al.. Engineering the ligand specificity of the human galectin-1 by incorporation of tryptophan analogs. ChemBioChem, Wiley-VCH Verlag, inPress, ⟨10.1002/cbic.202100593⟩. ⟨hal-03517502⟩

Share

Metrics

Record views

56

Files downloads

64