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19F Fast Magic-Angle Spinning NMR Spectroscopy on Microcrystalline Complexes of Fluorinated Ligands and the Carbohydrate Recognition Domain of Galectin-3

Kalabekova, Roza ; Quinn, Caitlin M. ; Movellan, Kumar Tekwani ; Gronenborn, Angela M. ; Akke, Mikael LU orcid and Polenova, Tatyana (2024) In Biochemistry 63(17). p.2207-2216
Abstract

Structural characterization of protein-ligand binding interfaces at atomic resolution is essential for improving the design of specific and potent inhibitors. Herein, we explored fast 19F- and 1H-detected magic angle spinning NMR spectroscopy to investigate the interaction between two fluorinated ligand diastereomers with the microcrystalline galectin-3 carbohydrate recognition domain. The detailed environment around the fluorine atoms was mapped by 2D 13C-19F and 1H-19F dipolar correlation experiments and permitted characterization of the binding interface. Our results demonstrate that 19F MAS NMR is a powerful tool for detailed characterization of... (More)

Structural characterization of protein-ligand binding interfaces at atomic resolution is essential for improving the design of specific and potent inhibitors. Herein, we explored fast 19F- and 1H-detected magic angle spinning NMR spectroscopy to investigate the interaction between two fluorinated ligand diastereomers with the microcrystalline galectin-3 carbohydrate recognition domain. The detailed environment around the fluorine atoms was mapped by 2D 13C-19F and 1H-19F dipolar correlation experiments and permitted characterization of the binding interface. Our results demonstrate that 19F MAS NMR is a powerful tool for detailed characterization of protein-ligand interfaces and protein interactions at the atomic level.

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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemistry
volume
63
issue
17
pages
10 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • scopus:85199053725
  • pmid:39008798
ISSN
0006-2960
DOI
10.1021/acs.biochem.4c00232
language
English
LU publication?
yes
id
bf8e3d65-fc2f-4fa5-a28c-fb00008a8f9a
date added to LUP
2024-11-14 09:30:10
date last changed
2025-02-06 17:12:14
@article{bf8e3d65-fc2f-4fa5-a28c-fb00008a8f9a,
  abstract     = {{<p>Structural characterization of protein-ligand binding interfaces at atomic resolution is essential for improving the design of specific and potent inhibitors. Herein, we explored fast <sup>19</sup>F- and <sup>1</sup>H-detected magic angle spinning NMR spectroscopy to investigate the interaction between two fluorinated ligand diastereomers with the microcrystalline galectin-3 carbohydrate recognition domain. The detailed environment around the fluorine atoms was mapped by 2D <sup>13</sup>C-<sup>19</sup>F and <sup>1</sup>H-<sup>19</sup>F dipolar correlation experiments and permitted characterization of the binding interface. Our results demonstrate that <sup>19</sup>F MAS NMR is a powerful tool for detailed characterization of protein-ligand interfaces and protein interactions at the atomic level.</p>}},
  author       = {{Kalabekova, Roza and Quinn, Caitlin M. and Movellan, Kumar Tekwani and Gronenborn, Angela M. and Akke, Mikael and Polenova, Tatyana}},
  issn         = {{0006-2960}},
  language     = {{eng}},
  month        = {{09}},
  number       = {{17}},
  pages        = {{2207--2216}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Biochemistry}},
  title        = {{<sup>19</sup>F Fast Magic-Angle Spinning NMR Spectroscopy on Microcrystalline Complexes of Fluorinated Ligands and the Carbohydrate Recognition Domain of Galectin-3}},
  url          = {{http://dx.doi.org/10.1021/acs.biochem.4c00232}},
  doi          = {{10.1021/acs.biochem.4c00232}},
  volume       = {{63}},
  year         = {{2024}},
}