A bivalent glycopeptide to target two putative carbohydrate binding sites on FimH

• Thisbe K. Lindhorst,
• Kathrin Bruegge,
• Andreas Fuchs and
• Oliver Sperling

Beilstein J. Org. Chem. 2010, 6, 801–809, doi:10.3762/bjoc.6.90

• fimbriated bacteria, respectively [13][14], multivalency effects were observed in many cases. In addition, concentration-dependent inhibitory and stimulating allosteric effects on adhesion have also been reported with certain carbohydrate ligands [15], which might be explained by the existence of allosteric

RAFT polymers for protein recognition

• Alan F. Tominey,
• Julia Liese,
• Sun Wei,
• Klaus Kowski,
• Thomas Schrader and
• Arno Kraft

Beilstein J. Org. Chem. 2010, 6, No. 66, doi:10.3762/bjoc.6.66

• protein enrichment and purification, sensing and diagnostics applications, as well as therapeutic uses involving interference with critical protein–protein interactions. Multivalency represents the key to generate high-affinity materials for biomacromolecules with a sufficient number of binding sites for

Synthesis in the glycosciences

• Thisbe K. Lindhorst

Beilstein J. Org. Chem. 2010, 6, No. 16, doi:10.3762/bjoc.6.16

• strategy where the glycosidic linkage is substituted by another type of ligation, or where glycosidations are limited to rather simple reactions whilst complexity and multivalency of a complicated target structure are introduced by alternative methods. Examples of such a versatile approach are also