Neo-Glycolipid Oximes as Intestinal Permeation Enhancers for Peptide Hormone PYY.

Herein, we describe the design and synthesis of 16 neo-glycolipids that are potential permeation enhancers for oral drug delivery of peptide therapeutics. These amphiphilic neo-glycolipids are composed of fatty acids and various carbohydrates (d-glucose, lactose, cellobiose, maltose) via an oxime linker. The ability of the synthesized neo-glycolipids to enhance permeation of fluorescein-labelled dextran (4 kDa) or H-mannitol across intestinal epithelium was investigated in vitro using monolayers of human epithelial Caco-2 cells.

Bioimaging and Biodistribution of the Metal-Ion-Controlled Self-Assembly of PYY Studied by SPECT/CT.

The controlled self-assembly of peptide- and protein-based pharmaceuticals is of central importance for their mode of action and tuning of their properties. Peptide YY (PYY ) is a 36-residue peptide hormone that reduces food intake when peripherally administered. Herein, we describe the synthesis of a PYY analogue functionalized with a metal-ion-binding 2,2'-bipyridine ligand that enables self-assembly through metal complexation.

Substrate specificity of novel GH16 endo-β-(1→3)-galactanases acting on linear and branched β-(1→3)-galactooligosaccharides.

Arabinogalactan proteins are proteoglycans located in the plant cell wall. Most arabinogalactan proteins are composed of carbohydrate moieties of β-(1→3)-galactan main chains with β-(1→6)-galactan side chains terminated by other glycans. In this study, three novel endo-β-(1→3)-galactanases were identified and the substrate specificity was further studied using well-defined galactan oligomers.