Glycopeptides

Synthetic glycopeptides offer a newly expanding frontier for research in glycobiology and proteomics as well as for drug discovery & development, drug delivery/targetting, diagnostics development and biotechnological applications.

The critical role of glycan elements on cell surface proteins and those bound to circulatory proteins is well 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 fragments (glycopeptides) as experimental probes for basic research and biomedical applications is growing rapidly.

The number and variation of applications of glycopeptides in modern research is impressive. Advanced Peptides 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 label if needed, and we will custom synthesize a molecule to your needs. 

Synthetic N-Linked Glycopeptides

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 are N-linked glycoproteins which contributes to increased in vivo half-life and bioavailability and hence higher therapeutic efficacy.

Synthetic O-linked Glycopeptides

Oxygen-linked glycopeptides and proteins are quite prevalent. Cell surface and extracellular proteins are O-glycosylated. 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 they 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.