Cover Feature: Altering the Modular Architecture of Galectins Affects its Binding with Synthetic α‐Dystroglycan O‐Mannosylated Core M1 Glycoconjugates In situ (ChemBioChem 14/2023)

Seek a cell anchorage galectin bridge: Transforming the wildtype Galectin (Gal)‐1 and ‐3 to a tandem‐repeat type variant via rational protein engineering enhanced cis‐binding activity with O‐Mannosylated core M1 glycopeptides of α‐dystroglycan (DG). Furthermore, the Gal‐1 variants (but not Gal‐3 var...

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Veröffentlicht in:Chembiochem : a European journal of chemical biology 2023-07, Vol.24 (14), p.n/a
Hauptverfasser: Villones, Lareno L., Ludwig, Anna‐Kristin, Kikuchi, Seiya, Ochi, Rika, Nishimura, Shin‐Ichiro, Gabius, Hans‐Joachim, Kaltner, Herbert, Hinou, Hiroshi
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Sprache:eng
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Zusammenfassung:Seek a cell anchorage galectin bridge: Transforming the wildtype Galectin (Gal)‐1 and ‐3 to a tandem‐repeat type variant via rational protein engineering enhanced cis‐binding activity with O‐Mannosylated core M1 glycopeptides of α‐dystroglycan (DG). Furthermore, the Gal‐1 variants (but not Gal‐3 variants) demonstrated trans‐bridging activity with the prepared α‐DG core‐M1 glycoconjugates and laminins in situ via the carbohydrate‐protein interactions. Thus, Gal‐1 and its variants are exciting candidates for treating several forms of muscular dystrophy. More information can be found in the Research Article by H. Kaltner, H. Hinou, et al.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.202300366