Elucidating the glycan-binding specificity and structure of Cucumis melo agglutinin, a new R-type lectin

• Jon Lundstrøm,
• Emilie Gillon,
• Valérie Chazalet,
• Nicole Kerekes,
• Antonio Di Maio,
• Ten Feizi,
• Yan Liu,
• Annabelle Varrot and
• Daniel Bojar

Beilstein J. Org. Chem. 2024, 20, 306–320, doi:10.3762/bjoc.20.31

• groundwork for further exploration of its biological and therapeutic potential. Keywords: carbohydrate; glycan array; melon; plant lectin; R-type; Introduction Lectins have long been the subject of intense scientific scrutiny, serving as molecular bridges that span the realms of biochemistry, cellular

High-affinity multivalent wheat germ agglutinin ligands by one-pot click reaction

• Henning S. G. Beckmann,
• Heiko M. Möller and
• Valentin Wittmann

Beilstein J. Org. Chem. 2012, 8, 819–826, doi:10.3762/bjoc.8.91

• conveniently prepared by employing a one-pot procedure for Cu(II)-catalyzed diazo transfer and Cu(I)-catalyzed azide–alkyne cycloaddition (CuAAC) starting from commercially available amines. These glycoclusters were probed for their binding potencies to the plant lectin wheat germ agglutinin (WGA) from

• ][29][30][31][32][33][34][35][36] or from screening of combinatorial libraries [37][38] have been reported. WGA is a 36 kDa plant lectin composed of two identical glycine- and cysteine-rich subunits [39] and is enriched in the seeds of Triticum vulgaris. It is specific for terminal N-acetylneuraminic