Download the Glycopeptides Product Brochure (2022)
Sussex Research Laboratories Inc. is the global leader in the field of glycopeptide synthesis and is the leading commercial source of synthetic, well-defined and characterized glycosylated peptides. We have been expanding our synthetic capabilities in the production of N- and O-linked glycopeptides for close to 20 years. We are also well-versed in the development of lipo, glyco-lipo, macrocyclic-, glycated (fructosylated), fluorescent/biotin-tagged and stable isotope-labelled glycopeptides and peptides.
GLYCOPEPTIDES FOR RESEARCH & DEVELOPMENT. Glycopeptides offer a unique frontier for research & development. Many critical roles of glycan elements on cell surface proteins and those bound to circulatory proteins are being recognized. Carbohydrates on proteins mediate a host of biological events including cell adhesion, immune system function, fertilization, cellular targeting as well as protein transport, stabilization, and half-life. Thus, the use of synthetic glycoproteins or their short glycopeptide fragments as experimental probes for basic research and biomedical applications is growing rapidly.
GLYCOPEPTIDES FOR DRUG DISCOVERY & DEVELOPMENT. Glycosylation of peptides is known to increase stability, solubility, in vivo half lives and ultimately, the efficacy of peptides in many cases. Glycosylation can impart very dramatic and beneficial biological effects in peptides and proteins. Short, stable, well characterized glycopeptide sequences taken from larger proteins can be highly potent ligands.
Glycopeptides from our Library: As the leading resource for glycopeptide synthesis, Sussex Research Laboratories Inc. offers a large number of glycopeptides from our inventory including but certainly not limited to:
Synthetic O-linked Glycopeptides
Oxygen-linked (O-linked) glycopeptides and proteins are highly prevalent on cell surfaces and extracellular proteins. The most abundant type of O-glycosylation in proteins is the N-acetylgalactosamine or alpha-GalNAc attachment to Ser or Thr in the protein chain. Most eukaryotic nuclear and cytoplasmic proteins are modified by N-acetylglucosamine (beta-O-GlcNAc) linked to Ser or Thr. Less prevalent types of O-glycosylation involve O-fucose (Fuc), O-mannose (Man) and O-glucose (Glc). However these are functionally of high relevance for early stages of development and for vital physiological functions of proteins. Glycosaminoglycans (GAG) are linked to proteoglycans via xylose (Xyl) linked to Ser.
Synthetic N-Linked Glycopeptides
Nitrogen-linked (N-linked) glycosylation is a post translational process that occurs in eukaryotes and widely in archaea but is rare in bacteria. It’s now understood that N-glycosylation plays a role in the folding of many eukaryotic proteins. Thus, approximately 70% of human therapeutic proteins contain N-linked glycans which contribute to increased in vivo half-life and bioavailability and hence higher therapeutic efficacy.
Peptide glycation results from non-enzymatic covalent attachment of sugars (particularly glucose) to proteins. Glycation often occurs at the N-terminal groups of proteins or at the side chains of lysines, arginines, cysteines, and histidines. Glycations occur mainly in the bloodstream concentrations of absorbed simple sugars such as glucose are high. Glycation end products are therefore implicated in many micro and macrovascular complications in diabetes, other diseases and in aging.
Custom Glycopeptide Synthesis
The number and variation in applications of glycopeptides in modern research is impressive. Sussex Research Laboratories Inc. is highly active in the custom synthesis of glycopeptides for specific research, drug, and vaccine development projects. You pick the glycoform, the amino acid or linker system, the sequence, and the probe or label if necessary, and we’ll make it happen.
Please browse our glycopeptide offering below.