Browse
Submit Data
Databases
API
Help

Dataset Information

33 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Automated glycan assembly using the Glyconeer 2.1 synthesizer.

ABSTRACT: Reliable and rapid access to defined biopolymers by automated DNA and peptide synthesis has fundamentally altered biological research and medical practice. Similarly, the procurement of defined glycans is key to establishing structure-activity relationships and thereby progress in the glycosciences. Here, we describe the rapid assembly of oligosaccharides using the commercially available Glyconeer 2.1 automated glycan synthesizer, monosaccharide building blocks, and a linker-functionalized polystyrene solid support. Purification and quality-control protocols for the oligosaccharide products have been standardized. Synthetic glycans prepared in this way are useful reagents as the basis for glycan arrays, diagnostics, and carbohydrate-based vaccines.

SUBMITTER: Hahm HS

PROVIDER: S-EPMC5410834 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

Automated glycan assembly using the Glyconeer 2.1 synthesizer.

Hahm Heung Sik HS Schlegel Mark K MK Hurevich Mattan M Eller Steffen S Schuhmacher Frank F Hofmann Johanna J Pagel Kevin K Seeberger Peter H PH

Proceedings of the National Academy of Sciences of the United States of America 20170410 17

Reliable and rapid access to defined biopolymers by automated DNA and peptide synthesis has fundamentally altered biological research and medical practice. Similarly, the procurement of defined glycans is key to establishing structure-activity relationships and thereby progress in the glycosciences. Here, we describe the rapid assembly of oligosaccharides using the commercially available Glyconeer 2.1 automated glycan synthesizer, monosaccharide building blocks, and a linker-functionalized polys ...[more]

PMID: 28396442

Similar Datasets

Microwave-Assisted Automated Glycan Assembly.

Project description:Automated synthesis of DNA, RNA, and peptides provides quickly and reliably important tools for biomedical research. Automated glycan assembly (AGA) is significantly more challenging, as highly branched carbohydrates require strict regio- and stereocontrol during synthesis. A new AGA synthesizer enables rapid temperature adjustment from -40 to +100 °C to control glycosylations at low temperature and accelerates capping, protecting group removal, and glycan modifications using elevated temperatures. Thereby, the temporary protecting group portfolio is extended from two to four orthogonal groups that give rise to oligosaccharides with up to four branches. In addition, sulfated glycans and unprotected glycans can be prepared. The new design reduces the typical coupling cycles from 100 to 60 min while expanding the range of accessible glycans. The instrument drastically shortens and generalizes the synthesis of carbohydrates for use in biomedical and material science.

| S-EPMC8213053 | biostudies-literature

Total Synthesis of Polysaccharides by Automated Glycan Assembly.

Project description:Polysaccharides are the most abundant biopolymers on earth that serve various structural and modulatory functions. Pure, completely defined linear and branched polysaccharides are essential to understand carbohydrate structure and function. Polysaccharide isolation provides heterogeneous mixtures, while heroic efforts were required to complete chemical and/or enzymatic syntheses of polysaccharides as long 92-mers. Here, we show that automated glycan assembly (AGA) enables access to a 100-mer polysaccharide via a 201-step synthesis within 188 h. Convergent block coupling of 30- and 31-mer oligosaccharide fragments, prepared by AGA, yielded a multiple-branched 151-mer polymannoside. Quick access to polysaccharides provides the basis for future material science applications of carbohydrates.

| S-EPMC7304863 | biostudies-literature

Automated glycan assembly of arabinomannan oligosaccharides from Mycobacterium tuberculosis.

Project description:Arabinomannan (AM) polysaccharides are clinical biomarkers for Mycobacterium tuberculosis (MTB) infections due to their roles in the interaction with host cells and interference with macrophage activation. Collections of defined AM oligosaccharides can help to improve the understanding of these polysaccharides and the development of novel therapeutical and diagnostic agents. Automated glycan assembly (AGA) was employed to prepare the core structure of AM from MTB, containing ?-(1,6)-Man, ?-(1,5)-Ara, and ?-(1,2)-Man linkages. The introduction of a capping step after each glycosylation and further optimized reaction conditions allowed for the synthesis of a series of oligosaccharides, ranging from hexa- to branched dodecasaccharides.

| S-EPMC6902893 | biostudies-literature

Systematic Structural Characterization of Chitooligosaccharides Enabled by Automated Glycan Assembly.

Project description:Chitin, a polymer composed of β(1-4)-linked N-acetyl-glucosamine monomers, and its partially deacetylated analogue chitosan, are abundant biopolymers with outstanding mechanical as well as elastic properties. Their degradation products, chitooligosaccharides (COS), can trigger the innate immune response in humans and plants. Both material and biological properties are dependent on polymer length, acetylation, as well as the pH. Without well-defined samples, a complete molecular description of these factors is still missing. Automated glycan assembly (AGA) enabled rapid access to synthetic well-defined COS. Chitin-cellulose hybrid oligomers were prepared as important tools for a systematic structural analysis. Intramolecular interactions, identified by molecular dynamics simulations and NMR analysis, underscore the importance of the chitosan amino group for the stabilization of specific geometries.

| S-EPMC7898498 | biostudies-literature

Enzymatic Building-Block Synthesis for Solid-Phase Automated Glycan Assembly.

Project description:Automated chemical oligosaccharide synthesis is an attractive concept that has been successfully applied to a large number of target structures, but requires excess quantities of suitably protected and activated building blocks. Herein we demonstrate the use of biocatalysis to supply such reagents for automated synthesis. By using the promiscuous NmLgtB-B β1-4 galactosyltransferase from Neisseria meningitidis we demonstrate fast and robust access to the LacNAc motif, common to many cell-surface glycans, starting from either lactose or sucrose as glycosyl donors. The enzymatic product was shown to be successfully incorporated as a complete unit into a tetrasaccharide target by automated assembly.

| S-EPMC7756758 | biostudies-literature

Automated glycan assembly of a S. pneumoniae serotype 3 CPS antigen.

Project description:Vaccines against S. pneumoniae, one of the most prevalent bacterial infections causing severe disease, rely on isolated capsular polysaccharide (CPS) that are conjugated to proteins. Such isolates contain a heterogeneous oligosaccharide mixture of different chain lengths and frame shifts. Access to defined synthetic S. pneumoniae CPS structures is desirable. Known syntheses of S. pneumoniae serotype 3 CPS rely on a time-consuming and low-yielding late-stage oxidation step, or use disaccharide building blocks which limits variability. Herein, we report the first iterative automated glycan assembly (AGA) of a conjugation-ready S. pneumoniae serotype 3 CPS trisaccharide. This oligosaccharide was assembled using a novel glucuronic acid building block to circumvent the need for a late-stage oxidation. The introduction of a washing step with the activator prior to each glycosylation cycle greatly increased the yields by neutralizing any residual base from deprotection steps in the synthetic cycle. This process improvement is applicable to AGA of many other oligosaccharides.

| S-EPMC4979738 | biostudies-literature

Automated glycan assembly of Lewis type I and II oligosaccharide antigens.

Project description:Human blood group related glycan antigens are fucosylated (neo-)lactoseries oligosaccharides that play crucial roles in pathogenic processes. Lewis type-II-chain antigens mark the surface of cancer cells, but are also mediators of bacterial infections. To investigate the biological roles of Lewis type glycans a host of synthetic approaches has been developed. Here, we illustrate how automated glycan assembly (AGA) using a set of six monosaccharide building blocks provides quick access to a series of more than ten defined Lewis type-I and type-II antigens, including Lex, Ley, Lea, Leb and KH-1. Glycans with up to three α-fucose branches were assembled following a strictly linear approach and obtained in excellent stereoselectivity and purity.

| S-EPMC6552968 | biostudies-literature

Automated Glycan Assembly of <sup>19</sup> F-labeled Glycan Probes Enables High-Throughput NMR Studies of Protein-Glycan Interactions.

Project description:Protein-glycan interactions mediate important biological processes, including pathogen host invasion and cellular communication. Herein, we showcase an expedite approach that integrates automated glycan assembly (AGA) of 19 F-labeled probes and high-throughput NMR methods, enabling the study of protein-glycan interactions. Synthetic Lewis type 2 antigens were screened against seven glycan binding proteins (GBPs), including DC-SIGN and BambL, respectively involved in HIV-1 and lung infections in immunocompromised patients, confirming the preference for fucosylated glycans (Lex , H type 2, Ley ). Previously unknown glycan-lectin weak interactions were detected, and thermodynamic data were obtained. Enzymatic reactions were monitored in real-time, delivering kinetic parameters. These results demonstrate the utility of AGA combined with 19 F NMR for the discovery and characterization of glycan-protein interactions, opening up new perspectives for 19 F-labeled complex glycans.

| S-EPMC8252726 | biostudies-literature

Automated glycan assembly of galactosylated xyloglucan oligosaccharides and their recognition by plant cell wall glycan-directed antibodies.

Project description:We report the automated glycan assembly of oligosaccharides related to the plant cell wall hemicellulosic polysaccharide xyloglucan. The synthesis of galactosylated xyloglucan oligosaccharides was enabled by introducing p-methoxybenzyl (PMB) as a temporary protecting group for automated glycan assembly. The generated oligosaccharides were printed as microarrays, and the binding of a collection of xyloglucan-directed monoclonal antibodies (mAbs) to the oligosaccharides was assessed. We also demonstrated that the printed glycans can be further enzymatically modified while appended to the microarray surface by Arabidopsis thaliana xyloglucan xylosyltransferase 2 (AtXXT2).

| S-EPMC6082630 | biostudies-literature

An automated synthesizer for electrochemical 18F-fluorination of organic compounds.

Project description:Electrochemical 18F-fluorination of organic compounds provides a means to synthesize Positron-Emission-Tomography (PET) tracers difficult to obtain otherwise. Here, the first automated synthesizer that enables radiolabeling through carrier-added electrochemical 18F-fluorination is described. The system provides capabilities for all necessary operations such as drying of cyclotron derived [18F]fluoride, electrochemical incorporation of the radioisotope into a precursor molecule, subsequent reactions such as protecting group removals, HPLC-purification and formulation of the final tracer. Demonstrated is the aliphatic electrochemical 18F-fluorination of methyl 2-(phenylthio)acetate.

| S-EPMC5585111 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data