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On the basis of extensive experience in peptide synthesis, Creative Peptides proudly offers the most comprehensive glycopeptides synthesis services to our worldwide clients. Our scientists are committed to deliver high quality glycopeptides which will go through strict mass spectral and HPLC analysis to meet our customers' demands.
In recently years, more and more attention has been focused on the function of glycopeptides in immunology realm. It is well-known that a majority of key molecules, which involved in innate and adaptive immune response, and some secondary metabolites produced by microorganism are all glycoeptides. And the glycosylation of immunoglobulins plays key roles in the regulation of immune reactions: glycans located at various sites modulate a diversity of immunoglobulin properties, including protein conformation, stability, serum half-life and binding affinity. In the meantime, changes in glycans or glycopeptides may also be involved in a variety of human immune-related diseases, such as rheumatoid, autoimmune disease, Wiskott-Aldrich syndrome, infection disease and even cancer. In this way, synthetic glycopeptides have provided a unique frontier for the investigation and better understanding in both glycobiology and proteomics, and also contribute to the development of either biotechnological or therapeutic applications.
Glycopeptides are a diverse and intricate class of biomolecules that play crucial roles in various biological processes. Comprising a peptide backbone adorned with complex carbohydrate moieties, glycopeptides exhibit remarkable structural diversity, contributing to their functional versatility. The term "glycopeptide" refers to the combined structure of the peptide/protein and the attached glycans.
Glycopeptide has been widely recognized as peptide that contains carbohydrate moieties (glycans). Due to the natural linkage between glycan and the amino acid residues of peptide, glycopeptides can be classified into three types: N-linked, O-linked and C-linked glycopeptides. Among them, N-linked glycopeptides are the most common type in nature, with N referring to the asparagine that attached by the glycan. Glycan of O-linked glycopeptides is commonly linked to the hydroxyl groups of serine and threonine, while sometimes also binding to lysine, proline and tyrosine. The least common C-linked glycopeptides are recognized as the attachment between mannose and tryptophane.
Based on Glycan Attachment Site, glycopeptides can be classified into three types: N-Terminal, Internal, and C-Terminal glycopeptides. N-Terminal Glycopeptides have glycan attachments at the N-terminus of the peptide chain. Internal Glycopeptides have glycan attachments within the peptide sequence, usually at specific asparagine or serine/threonine residues. C-Terminal Glycopeptides have glycan attachments at the C-terminus of the peptide chain.
Cellular Recognition and Signaling: Glycopeptides play a crucial role in cell recognition and signaling processes. The glycan structures on cell surface glycoproteins act as recognition motifs, facilitating interactions with other cells or extracellular molecules. These interactions are involved in critical biological processes such as immune response, cell adhesion, migration, and tissue organization.
Immunology and Vaccines: Glycopeptides are key components in the development of glycopeptide-based vaccines. By incorporating pathogen-specific glycan antigens, vaccines can induce a targeted immune response. Glycopeptide-based vaccines have shown promise in generating protective antibodies against pathogens and can potentially be used for the prevention and treatment of infectious diseases.
Antibiotics: Antibiotic glycopeptides, such as vancomycin and teicoplanin, are widely used in clinical settings to combat bacterial infections. These glycopeptides inhibit bacterial cell wall synthesis by binding to specific targets, making them effective against Gram-positive bacteria. However, the emergence of antibiotic resistance poses a challenge, necessitating the development of new glycopeptide antibiotics or alternative approaches.
Biomarkers and Diagnostics: Glycopeptides and their associated glycans can serve as biomarkers for various diseases, including cancer and genetic disorders. Alterations in glycosylation patterns are often associated with disease states, making glycopeptides valuable diagnostic markers. Detection and analysis of glycopeptide biomarkers can provide insights into disease progression, aid in early detection, and guide personalized medicine approaches.
Glycopeptides, especially the glycan chains, have played pivotal roles in various biological activities and involved in numerous biological recognition events, such as immune system, endocrine system, protein folding and cell communication. There are three major roles of the glycans:
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