Glycopeptides offer a unique frontier for research & development. 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.
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Learn more about Glycopeptides & Peptides
At Sussex Research Laboratories Inc., we stand at the cutting edge of glycopeptide synthesis, cementing our status as the world's leading provider of synthetic, precisely defined, and characterized glycosylated peptides. With nearly two decades of dedicated effort, we have refined our synthesis techniques to master both N- and O-linked glycopeptides. Our expertise does not end there; we specialize in a broad spectrum of peptides including lipopeptides, glycolipopeptides, macrocyclic peptides, fructosylated peptides, and peptides tagged with fluorescent or biotin markers, as well as peptides labeled with stable isotopes.
Unlocking Potentials in Research & Development
Glycopeptides are revolutionizing the research and development landscape, highlighting the critical roles of glycans in cell-surface and circulatory proteins. These carbohydrates are pivotal in various biological processes such as cell adhesion, immune responses, fertilization, and cellular targeting. They are essential for the transport, stabilization, and lifespan of proteins. Consequently, synthetic glycoproteins and glycopeptide fragments have become indispensable tools for fundamental research and biomedical applications, witnessing a swift expansion in their usage.
Advancing Drug Discovery & Development
The glycosylation of peptides considerably enhances their stability, solubility, and bioavailability, often amplifying the effectiveness of peptide-based therapies. Such modifications endow peptides and proteins with beneficial biological properties, making short, stable, and well-characterized glycopeptide sequences derived from larger proteins highly efficient as ligands.
Our Glycopeptide Expertise
As a frontrunner in glycopeptide synthesis, we boast an extensive expertise in glycopeptides, including but not limited to:
Mucins like MUC1 and glycopeptides associated with cancer
Erythropoietin analogs
Fragments of the RNA polymerase II C-Terminal Domain
Glycopeptides from the IgA Hinge domain
PSGL-1 mimetics
Frizzled 8 analogs (FRZD8 or Antiproliferative factor)
O-GlcNAc-modified nucleocytoplasmic protein fragments
Glycated hemoglobin fragments
Synthetic O-Linked Glycopeptides
O-linked glycopeptides and proteins, essential on cell surfaces and in extracellular proteins, predominantly involve the attachment of N-acetylgalactosamine (alpha-GalNAc) to Ser or Thr. Other types of O-glycosylation, crucial in early development and protein functions, are also a part of our repertoire.
Synthetic N-Linked Glycopeptides
N-linked glycosylation, a key post-translational modification in eukaryotes and archaea, is instrumental in protein folding. A significant portion of human therapeutic proteins, benefiting from increased in vivo half-life and bioavailability due to N-linked glycans, contains these modifications.
Glycated Peptides
Peptide glycation, the non-enzymatic attachment of sugars to proteins, is a process implicated in various complications associated with diabetes, aging, and other conditions. This area is another expertise of ours, highlighting our comprehensive capabilities in glycopeptide synthesis.
TKLSQKFTKVN*FTEIQKLVLDC-NH2
where N* = Asn* = GlcNAcβ-N-Asn
AFP(241-261-Cys)-GlcNAc(251)
Product #: GP200080
UniProt ID: P02771
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Ac-KILRTQESECVCS*-NH2
where S* = Ser* = GlcNAcβ-O-Ser
Ac-Lys-Neuraminidase(219-230)-GlcNAc(230)-Influenza A virus
Product #: GP200085
UniProt ID: I3PAZ0
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K(CNTATC)ATQRLANFLVHSSNNFGPILLPPTNVGSNTY-NH2
Amylin(34-71)-Synthetic Analogue
Product #: GP200100
UniProt ID: P10997
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K(CNTATC)ATQRLANFLVHSSNNFGPILLPPTN*VGSNTY-NH2
Where N* = Asn* = GlcNAcβ-Asn
Amylin(34-71)-GlcNAc(69)-Synthetic Analogue
Product #: GP200101
UniProt ID: P10997
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K(CNTATC)ATQRLANFLVHSSNNFGPILLPPTN*VGSNTY-NH2
Where N* = Asn* = GlcNAcβ-Asn
Amylin(34-71)-GlcNAc(65)-Synthetic Analogue
Product #: GP200102
UniProt ID: P10997
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Fructosyl-VHLTPE-OH
HBB(2-7)-Fructose
Product #: GP300000
UniProt ID: P68871
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Fructosyl-VHLTPEC-NH2
HBB(2-7-Cys)-Fru(2)
Product #: GP300005
UniProt ID: P68871
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Fructosyl-VHLTPEEKSC-NH2
HBB(2-10-Cys)-Fru(2)
Product #: GP300010
UniProt ID: P68871
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VHLTPEEKSC-NH2
HBB(2-10-Cys)-ng
Product #: GP300011
UniProt ID: P68871
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Fructosyl-VH(PEG)C-NH2
Synthetic Glycopeptide 4
Product #: GP300015
UniProt ID: N/A
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Fruc-VHLTC-NH2
HBB(2-5-Cys)-Fru(2)
Product #: GP300020
UniProt ID: P68871
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VHLTC-NH2
HBB(2-5-Cys)
Product #: GP300021
UniProt ID: P68871
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TPRVERN*GHSVFLAPYGWMVK-OH
where N* = Asn* = Glcβ-N-Asn
Synthetic Glycopeptide 5
Product #: GP500000
UniProt ID: N/A
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YaFE-Nle-Nle-T*-NH2
where T* = Thr* = Glcβ-O-Thr
Synthetic Glycopeptide 6
Product #: GP500005
UniProt ID: N/A
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Ac-KILRTQESECVCS*-NH2
where S* = Ser* = Glcβ-O-Ser
Ac-Lys-Neuraminidase(219-230)-Glc(230)-Influenza A virus