Sugar is an important nutrient for the human body, and its primary physiological function is to provide energy and carbon sources for life activities. In addition, sugar also participates in the composition of glycoproteins and glycolipids, and regulates cell information transmission. Monosaccharides are polymerized by glycosidic bonds to form oligosaccharides or polysaccharides, also called glycans. Glycans are covalently linked with proteins or lipids to form complex biological macromolecules, which are divided into glycoproteins, proteoglycans and glycolipids, also known as sugar complexes.
Glycans in glycoprotein molecules
Glycoprotein is formed by carbohydrate molecules that covalently bond with protein molecules. There are 7 kinds of monosaccharides that make up glycans in the glycoprotein molecules: glucose, galactose, mannose, N-acetylgalactosamine, N-acetylglucosamine, fucose, and N-acetylneuraminic acid.
According to the different ways of connection with proteins, glycoproteins can be categorized as N-linked glycans and O-linked glycans. N-linked glycans are linked to the amide nitrogen of asparagine residues in protein molecules. O-linked glycans are connected to the serine or threonine hydroxyl groups in protein molecules. The synthesis of N-linked glycan uses long terpene alcohol as a glycan carrier, while O-linked glycan synthesis does not require a glycan carrier. Statistically, about one-third of the proteins in human cells are glycoproteins and perform different functions. Glycans in glycoprotein molecules can affect the conformation, polymerization, dissolution and degradation of the protein part and participate in the mutual recognition and binding of glycoproteins.
Glycosaminoglycans in proteoglycan molecules
Proteoglycans are dominated by glycan content, and glycosaminoglycans are covalently linked to different core proteins to form sugar complexes. Glycosaminoglycans are heteropolysaccharides formed by the repeated connection of disaccharide units without branching. One of the disaccharide units is glycosamine (N-acetylglucosamine or N-acetylgalactosamine) and the other is uronic acid (glucuronic acid or iduronic acid). There are six essential glycosaminoglycans in the body: chondroitin sulfate, dermatan sulfate, keratan sulfate, hyaluronic acid, heparin, and heparan sulfate. These glycosaminoglycans are composed of repeating disaccharide units. Except for hyaluronic acid, all other glycosaminoglycans contain sulfuric acid. Moreover, the protein that is covalently bound to the glycosaminoglycan chain is called the core protein. Core proteins contain corresponding glycosaminoglycan substitution domains, and some proteoglycans are anchored to the cell surface or extracellular matrix macromolecules through unique domains of the core protein. The primary function of proteoglycan is to form the intercellular matrix, which can bind to the hyaluronic acid receptor on the cell surface and affect cell-to-cell adhesion, migration, proliferation and differentiation.
Glycolipid
Glycolipids are complex lipids that carry one or more covalently linked sugar groups. Due to the difference in lipids, glycolipids can be divided into sphingomyelin, glyceroglycolipid and steroid-derived glycolipid. Like sphingomyelin, glycosphingolipids are compounds based on ceramide. The ceramide 1-hydroxyl group in the sphingomyelin molecule is aminated by phosphatidylcholine or phosphatidylethanol, while ceramide 1-hydroxyl group in the glycosphingolipid molecule is glycosylated to form a glycoside compound. Furthermore, the monosaccharides in glycosphingolipid molecules are mainly composed of D-glucose, D-galactose, N-acetylglucosamine, N-acetylgalactosamine, fucose and sialic acid. Glycosphingolipids can be divided into neutral glycosphingolipids and acidic glycosphingolipids according to whether the molecule contains sialic acid or sulfate-based components. For example, cerebrosides are neutral glycosphingolipids without the sialic acid, and gangliosides are acid glycosphingolipids containing sialic acid.
Glycans are involved in cell recognition, cell adhesion, cell differentiation, immune recognition, signal transduction, microbial pathogenic processes and tumor metastasis processes. Creative Proteomics reserved extensive experience in glycomics research, and can provide customized glycan analysis services for customers in many regions and countries.
Reference
Costa, A. F., Campos, D., Reis, C. A., & Gomes, C. (2020). Targeting glycosylation: a new road for cancer drug discovery. Trends in cancer, 6(9), 757-766.
The rapidly growing pipeline of recombinant glycoprotein therapeutics, especially the glycoengineered variants of COVID-19 drugs, has presented lucrative opportunities for contract service providers with expertise in glycoconjugate / glycan analysis Roots Analysis is pleased to announce the publication of its recent study, titled, “Glycosylation Analysis Services Market, 2021 – 2030” To order this 310+ page report, which features 80+ figures and 130+ tables, please visit https://www.rootsanalysis.com/reports/glycosylation-analysis-services-market.html The report features an extensive study on the current market landscape, offering an informed opinion on the likely evolution of the market, over the next decade.
Amongst other elements, the report includes:A detailed review of the overall landscape of the glycan analysis services market, highlighting the contributions of industry players, along with the information on their year of establishment, company size, geographical location of headquarters, type of service(s) offered (glycan profiling and heterogeneity analysis, glycosylation site mapping and occupancy analysis, site- specific glycosylation analysis, glycan structure analysis, monosaccharide quantification analysis and protein- glycan binding analysis), type of glycoconjugate and glycan analyzed (N- glycan, O- glycan and glycolipid), type of sample analyzed (biotherapeutics and cellular), type of analyte processed (intact glycoprotein, glycopeptide, released glycan, monosaccharide and polysaccharide), type of analytical technique used (chromatography, spectroscopy, electrophoresis and microarray- based technique), application area (R / early- stage drug development and in- process drug development) It also provides information on the additional services offered (peptide mapping, post- translational modification analysis, protein terminal sequencing and glycan / glycoconjugate synthesis), and availability of synthetic glycans and analytical kits / tests.
In addition, it provides information on the type of glycoanalytical service offered and type of technique used by non-industry players.A region-wise company competitiveness analysis, highlighting the most prominent glycan analysis service providers, based on their supplier strength (in terms of experience and company size), and portfolio specifications (in terms of number of services offered, number of analytical techniques used, types of glycans analyzed, types of analytes processed and applications).Elaborate profiles of prominent service providers in this domain.
Each company profile includes a brief overview of the company, its financial information (if available), information on service portfolio, recent developments, and an informed future outlook.A detailed assessment of the current market landscape of surface glycan targeting therapeutics, providing information on the phase of development (commercial, clinical, preclinical, and discovery) of lead candidates, target disease indication and therapeutic area, type of drug molecule (antibody, antibody-drug conjugate, enzyme, glyco- conjugate vaccine and CAR- T cells), target glycan / glycoconjugate molecule, type of therapy (monotherapy, combination therapy and both), and technology platform used.
In addition, it provides details on drug developer(s), including information on their year of establishment, company size, and location of headquarters.A detailed analysis of grants that have been awarded to research institutes for surface glycan targeting therapeutic projects, during the period, 2016 and 2021, based on several relevant parameters, such as year of grant award, amount awarded, administering institute center, support period, type of grant application, purpose of grant award, activity code, study section involved, type of recipient organizations and focus area.
In addition, it highlights geographical distribution of recipient organizations, popular funding institute centers, prominent program officers, and popular recipient organizations.An analysis of the partnerships that have been established in this domain since 2015, covering instances of acquisitions and mergers, licensing agreements, product development agreements, process development agreement, research agreements, and other relevant types of deals.A detailed analysis of the various mergers and acquisitions that have taken place in this domain, highlighting the trend in the number of companies acquired during the time period between 2015- 2021, based on several relevant parameters, such as year of agreement, type of deal, geographical location of headquarters, company size, and the key value drivers.
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