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Search for "lectins" in Full Text gives 56 result(s) in Beilstein Journal of Organic Chemistry.

An easily accessible sulfated saccharide mimetic inhibits in vitro human tumor cell adhesion and angiogenesis of vascular endothelial cells

  • Grazia Marano,
  • Claas Gronewold,
  • Martin Frank,
  • Anette Merling,
  • Christian Kliem,
  • Sandra Sauer,
  • Manfred Wiessler,
  • Eva Frei and
  • Reinhard Schwartz-Albiez

Beilstein J. Org. Chem. 2012, 8, 787–803, doi:10.3762/bjoc.8.89

Graphical Abstract
  • among cells are mediated by binding of proteins such as lectins to oligosaccharides. Upon progression to higher malignancy, the glycosylation patterns of glycoproteins and glycosphingolipids on tumor cell surfaces undergo several alterations [6]. These changes are closely associated with distinct
  • oligosaccharides and lectins, by synthetic carbohydrate analogues [10][11][12][13]. Based on Schmidt’s imidate strategy [14], we have developed a method for the synthesis of a library of saccharide-mimetics containing furans. Furan, especially as its bis-hydroxymethylated derivative, was chosen as a core molecule
  • ]. Furthermore, the overexpression of the charged blood group antigen sialyl Lewisx consisting of the terminal NeuNAcα2-3Galβ1-4(Fucα1-3)GlcNAc-group is correlated with carcinogenesis. It is recognized and bound by selectins, which are a subgroup of lectins that play an important role as cell-surface molecules
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Published 29 May 2012

Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment

  • Christiane E. Kupper,
  • Ruben R. Rosencrantz,
  • Birgit Henßen,
  • Helena Pelantová,
  • Stephan Thönes,
  • Anna Drozdová,
  • Vladimir Křen and
  • Lothar Elling

Beilstein J. Org. Chem. 2012, 8, 712–725, doi:10.3762/bjoc.8.80

Graphical Abstract
  • epitopes on glycoproteins and glycolipids are based on N-acetyllactosamine units (LacNAc; Galβ1,4GlcNAc) and often present on extended poly-LacNAc glycans ([Galβ1,4GlcNAc]n). Poly-LacNAc itself has been identified as a binding motif of galectins, an important class of lectins with functions in immune
  • ][5]. Poly-LacNAc itself was identified as a recognition motif of galectins, which are an important class of mammalian lectins [6][7]. Another LacNAc related epitope is LacDiNAc (GalNAcβ1,4GlcNAc), which is especially well-known from parasitic nematodes and trematodes [8][9]. In humans, LacDiNAc
  • reaction mixture leads to the formation of α,β-unsaturated aldehydes. By branching, the avidity of glycans has been shown to increase, which is important for the binding affinity of lectins [56][57]. The chemically branched poly-LacNAc glycans may, moreover, serve as analogues to naturally occurring I
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Published 09 May 2012

Amine-linked diglycosides: Synthesis facilitated by the enhanced reactivity of allylic electrophiles, and glycosidase inhibition assays

  • Ian Cumpstey,
  • Jens Frigell,
  • Elias Pershagen,
  • Tashfeen Akhtar,
  • Elena Moreno-Clavijo,
  • Inmaculada Robina,
  • Dominic S. Alonzi and
  • Terry D. Butters

Beilstein J. Org. Chem. 2011, 7, 1115–1123, doi:10.3762/bjoc.7.128

Graphical Abstract
  • disaccharide mimicry. Last year, we reported that neutral ether- and thioether-linked diglycose derivatives can interact with lectins with affinities similar to those of strongly binding disaccharide ligands [4]. In the related carbasugar series, Ogawa et al. have shown that pseudodisaccharides with a bridging
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Published 16 Aug 2011

En route to photoaffinity labeling of the bacterial lectin FimH

  • Thisbe K. Lindhorst,
  • Michaela Märten,
  • Andreas Fuchs and
  • Stefan D. Knight

Beilstein J. Org. Chem. 2010, 6, 810–822, doi:10.3762/bjoc.6.91

Graphical Abstract
  • shown both by MS/MS studies and by affino dot–blot analysis. Keywords: diazirines; FimH; lectins; MS/MS analysis; photoactive mannoside ligands; photoaffinity labeling; Introduction Photoaffinity labeling is a technique by which ligand binding sites of a receptor protein can be identified in solution
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Published 26 Aug 2010

New amphiphilic glycopolymers by click functionalization of random copolymers – application to the colloidal stabilisation of polymer nanoparticles and their interaction with concanavalin A lectin

  • Otman Otman,
  • Paul Boullanger,
  • Eric Drockenmuller and
  • Thierry Hamaide

Beilstein J. Org. Chem. 2010, 6, No. 58, doi:10.3762/bjoc.6.58

Graphical Abstract
  • . These copolymers are water soluble. Recognition of PCL nanoparticles by concanavalin A Lectins are proteins of non-immunological origin, able to bind carbohydrate ligands, without any enzymatic or immunological function. They are multivalent and can bind several ligands simultaneously and participate in
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Published 01 Jun 2010

Dimerization of propargyl and homopropargyl 6-azido- 6-deoxy- glycosides upon 1,3-dipolar cycloaddition

  • Nikolas Pietrzik,
  • Daniel Schmollinger and
  • Thomas Ziegler

Beilstein J. Org. Chem. 2008, 4, No. 30, doi:10.3762/bjoc.4.30

Graphical Abstract
  • libraries of highly glycosylated peptides, some members of which were indeed shown to behave like oligosaccharide mimics capable to specifically bind lectins [1][4]. In order to increase the structural diversity of the aforementioned building blocks, we contemplated using as the spacer entity 1,2,3
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Published 13 Aug 2008
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