Fluorine (19F) incorporation into glycan-binding proteins (lectins) has been achieved and exploited to monitor the binding to carbohydrate ligands by nuclear magnetic resonance (NMR) spectroscopy. Galectins are a family of lectins that bind carbohydrates, generally with weak affinities, through a combination of intermolecular interactions including a key CH-π stacking involving a conserved tryptophan residue. Herein, Galectin-3 (Gal3) and Galectin-8 (Gal8) with one and two carbohydrate recognition domains (CRDs), respectively, were selected. Gal3 contains one Trp, whereas Gal8 contains three, one at each binding site and a third one not involved in sugar binding; these were substituted by the corresponding F-Trp analogues. The presence of fluorine did not significantly modify the affinity for glycan binding, which was in slow exchange on the 19F NMR chemical-shift timescale, even for weak ligands, and allowed binding events taking place at two different binding sites within the same lectin to be individualized.

Lete, M., Franconetti, A., Bertuzzi, S., Delgado, S., Azkargorta, M., Elortza, F., et al. (2023). NMR Investigation of Protein-Carbohydrate Interactions: The Recognition of Glycans by Galectins Engineered with Fluorotryptophan Residues. CHEMISTRY-A EUROPEAN JOURNAL, 29(5) [10.1002/chem.202202208].

NMR Investigation of Protein-Carbohydrate Interactions: The Recognition of Glycans by Galectins Engineered with Fluorotryptophan Residues

Bertuzzi S.;
2023

Abstract

Fluorine (19F) incorporation into glycan-binding proteins (lectins) has been achieved and exploited to monitor the binding to carbohydrate ligands by nuclear magnetic resonance (NMR) spectroscopy. Galectins are a family of lectins that bind carbohydrates, generally with weak affinities, through a combination of intermolecular interactions including a key CH-π stacking involving a conserved tryptophan residue. Herein, Galectin-3 (Gal3) and Galectin-8 (Gal8) with one and two carbohydrate recognition domains (CRDs), respectively, were selected. Gal3 contains one Trp, whereas Gal8 contains three, one at each binding site and a third one not involved in sugar binding; these were substituted by the corresponding F-Trp analogues. The presence of fluorine did not significantly modify the affinity for glycan binding, which was in slow exchange on the 19F NMR chemical-shift timescale, even for weak ligands, and allowed binding events taking place at two different binding sites within the same lectin to be individualized.
Articolo in rivista - Articolo scientifico
19; F NMR spectroscopy; engineered galectins; fluorotryptophan; glycans; molecular recognition;
English
7-nov-2022
2023
29
5
e202202208
open
Lete, M., Franconetti, A., Bertuzzi, S., Delgado, S., Azkargorta, M., Elortza, F., et al. (2023). NMR Investigation of Protein-Carbohydrate Interactions: The Recognition of Glycans by Galectins Engineered with Fluorotryptophan Residues. CHEMISTRY-A EUROPEAN JOURNAL, 29(5) [10.1002/chem.202202208].
File in questo prodotto:
File Dimensione Formato  
Lete-2023-Chemistry A European J-VOR.pdf

accesso aperto

Descrizione: CC BY-NC-ND 4.0 This is an open access article under the terms of the Creative Commons Attribution Non-Commercial NoDerivs License
Tipologia di allegato: Publisher’s Version (Version of Record, VoR)
Licenza: Creative Commons
Dimensione 3.58 MB
Formato Adobe PDF
3.58 MB Adobe PDF Visualizza/Apri

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/512779
Citazioni
  • Scopus 1
  • ???jsp.display-item.citation.isi??? 1
Social impact