Molecular architecture with carbohydrate functionalized β-peptides adopting 3₁₄-helical conformation

• Nitin J. Pawar,
• Navdeep S. Sidhu,
• George M. Sheldrick,
• Dilip D. Dhavale and
• Ulf Diederichsen

Beilstein J. Org. Chem. 2014, 10, 948–955, doi:10.3762/bjoc.10.93

• conformationally constrained and well-defined scaffold for sugar presentation on a 314-helix [18][19][20] as well as on a β-peptide 312-helical scaffold obtained by oligomerization of glycosylated pyrrolidine β-amino acids [35]. Glycopeptide or glycoprotein synthesis is challenged by different conditions required

Synthetic glycopeptides and glycoproteins with applications in biological research

• Ulrika Westerlind

Beilstein J. Org. Chem. 2012, 8, 804–818, doi:10.3762/bjoc.8.90

• backbones, or mimics thereof, offer further possibilities to study protein-binding events. Keywords: glycopeptide binding; glycopeptides; glycoprotein synthesis; solid-phase peptide synthesis; synthetic vaccines; Introduction The majority of human proteins are co- or post-translationally modified by mono

• techniques for glycoprotein synthesis by preparation of a number of GalNAc containing O-glycoproteins, such as the antimicrobial protein diptericin, the cytokine lymphotactin and the leukocyte adhesion molecule ligand GlyCAM-1 [46][47][48]. By repeated NCL couplings of mucin tandem repeats, MUC2 and MUC1

• reported to stay intact (Scheme 5) [70][78]. Although applicable in glycopeptide ligation, the Tmb auxiliary strategy is of limited use in glycoprotein synthesis, due to the harsh conditions employed for auxiliary removal. Furthermore, due to steric hindrance by the auxiliary group, the reactivity of the