Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Thio-mediated synthesis of derivatized N-linked glycopeptides using isonitrile chemistry.

ABSTRACT: The reaction of oligosaccharide isonitriles with peptide thioacids in the presence of bulky thiophenol as activator to provide N-linked glycopeptides at room temperature is described.

SUBMITTER: Wu X

PROVIDER: S-EPMC2735058 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

Thio-mediated synthesis of derivatized N-linked glycopeptides using isonitrile chemistry.

Wu Xiangyang X Yuan Yu Y Li Xuechen X Danishefsky Samuel J SJ

Tetrahedron letters 20090801 32

The reaction of oligosaccharide isonitriles with peptide thioacids in the presence of bulky thiophenol as activator to provide N-linked glycopeptides at room temperature is described. ...[more]

PMID: 20161157

Similar Datasets

Isonitrile-Derivatized Indole as an Infrared Probe for Hydrogen-Bonding Environments.

Project description:The isonitrile (NC) group has been shown to be a promising infrared probe for studying the structure and dynamics of biomolecules. However, there have been no systematic studies performed on the NC group as an infrared probe, when it is bonded to an indole ring. Here, we systematically study the NC stretching mode of two model compounds, 5-isocyano-1H-indole (5ICI) and 5-isocyano-1-methyl-1H-indole (NM5ICI), using Fourier transform infrared (FTIR) spectroscopy. The NC stretching frequency is shown to be strongly dependent on the polarizability of protic solvents and the density of hydrogen-bond donor groups in the solvent when NC is bonded to an indole ring. Infrared pump⁻probe studies of 5ICI in DMSO and in EtOH further support that the NC stretching mode could be used as a site-specific infrared probe for local environments when NC is bonded to an indole ring.

| S-EPMC6480494 | biostudies-literature

Capture and release of alkyne-derivatized glycerophospholipids using cobalt chemistry.

Project description:Alkyne-modified phospholipids can be unambiguously identified and differentiated from native species in complex mixtures by formation of dicobalthexacarbonyl complexes. This reaction is specific for alkynes and is unaffected by other glycerophospholipid-related moieties. Enrichment of cells with alkyne-derivatized fatty acids or glycerophospholipids followed by solid-phase sequestration and release is a promising new method for unequivocally monitoring individual glycerophospholipids following incorporation into cells. This technique also facilitates lipidomic analysis of substrates and products.

| S-EPMC2822082 | biostudies-literature

Peptidyl ?-Asp Selenoesters Enable Efficient Synthesis of N-Linked Glycopeptides.

Project description:Chemical synthesis is an attractive approach allows for the assembly of homogeneous complex N-linked glycopeptides and glycoproteins, but the limited coupling efficiency between glycans and peptides hampered the synthesis and research in the related field. Herein we developed an alternative glycosylation to construct N-linked glycopeptide via efficient selenoester-assisted aminolysis, which employs the peptidyl ?-asparagine selenoester and unprotected glycosylamine to perform rapid amide-bond ligation. This glycosylation strategy is highly compatible with the free carboxylic acids and hydroxyl groups of peptides and carbohydrates, and readily available for the assembly of structure-defined homogeneous N-linked glycopeptides, such as segments derived from glycoprotein EPO and IL-5.

| S-EPMC7232547 | biostudies-literature

Chemoselective Solution- and Solid-Phase Synthesis of Disulfide-Linked Glycopeptides.

Project description:Glycosylation of peptides and proteins is a widely employed strategy to mimic important post-translational modifications or to modulate the physicochemical properties of peptides to enhance their delivery. Furthermore, glycosylation via a sulfur atom imparts increased chemical and metabolic stability to the resulting glycoconjugates. Herein, we report a simple and chemoselective procedure to prepare disulfide-linked glycopeptides. Acetate-protected glycosylsulfenyl hydrazines are shown to be highly reactive with the thiol group of cysteine residues within peptides, both in solution and as part of conventional solid-phase peptide synthesis protocols. The efficiency of this glycosylation methodology with unprotected carbohydrates is also demonstrated, which avoids the need for deprotection steps and further extends its utility, with disulfide-linked glycopeptides produced in excellent yields. Given the importance of glycosylated peptides in structural glycobiology, pharmacology, and therapeutics, the methodology outlined provides easy access to disulfide-linked glycopeptides as molecules with multiple biological applications.

| S-EPMC9638999 | biostudies-literature

Metabolic glycan imaging by isonitrile-tetrazine click chemistry.

Project description:Seeing the sugar coating: N-Acetyl-glucosamine and mannosamine derivatives tagged with an isonitrile group are metabolically incorporated into cell-surface glycans and can be detected with a fluorescent tetrazine. This bioorthogonal isonitrile-tetrazine ligation is also orthogonal to the commonly used azide-cyclooctyne ligation, and so will allow simultaneous detection of the incorporation of two different sugars.

| S-EPMC3743162 | biostudies-literature

On the synthesis of conformationally modified peptides through isonitrile chemistry: implications for dealing with polypeptide aggregation.

Project description:A method for introducing a dimethyleneoxy constraint joining the N atoms of two consecutive amino acids in the context of a polypeptide has been developed. This constraint can profoundly affect the tendency of a polypeptide to suffer aggregation and desolubilization, and it can be readily removed under mild conditions.

| S-EPMC3108857 | biostudies-literature

Facile triflic acid-catalyzed ?-1,2-cis-thio glycosylations: scope and application to the synthesis of S-linked oligosaccharides, glycolipids, sublancin glycopeptides, and TN/TF antigens.

Project description:Studies of S-linked glycoconjugates have attracted growing interest because of their enhanced chemical stability and enzymatic resistance over O-glycoside counterparts. We here report a facile approach to access ?-1,2-cis-S-linked glycosides using triflic acid as a catalyst to promote the glycosylation of a series of thiols with d-glucosamine, galactosamine, glucose, and galactose electrophiles. This method is broadly applicable for the stereoselective synthesis of S-linked glycopeptides, oligosaccharides and glycolipids in high yield and excellent ?-selectivity. Many of the synthetic limitations associated with the preparation of these S-linked products are overcome by this catalytic method.

| S-EPMC7020787 | biostudies-literature

Solid phase extraction of N-linked glycopeptides using hydrazide tip.

Project description:Glycoproteome contains valuable information where biomarkers may be discovered for disease diagnosis and monitoring. Nowadays, with the ever-increasing performances of mass spectrometers, the emphasis is shifting to the sample preparation for better throughput and reproducibility. Therefore, to facilitate high throughput N-linked glycopeptide isolation, in this study, a novel hydrazide tip was devised and an integrated workflow of N-linked glycopeptide isolation using hydrazide tips was presented. With the use of bovine fetuin as a standard glycoprotein, the incubation time was determined for each major step of glycopeptide isolation. With the use of commercially available human serum, multiple parallel isolations of glycopeptides were performed using hydrazide tips with a liquid handling robotic system. We demonstrated that, with the hydrazide tips, the processing time was significantly decreased from 3 to 4 days to less than 8 h with excellent reproducibility. The hydrazide pipet tips have great potential in achieving automation of N-linked glycopeptide isolation for high-throughput sample preparation when used in combination with liquid handling robotic systems.

| S-EPMC4082910 | biostudies-literature

Characterization of intact N- and O-linked glycopeptides using higher energy collisional dissociation.

Project description:Simultaneous elucidation of the glycan structure and the glycosylation site are needed to reveal the biological function of protein glycosylation. In this study, we employed a recent type of fragmentation termed higher energy collisional dissociation (HCD) to examine fragmentation patterns of intact glycopeptides generated from a mixture of standard glycosylated proteins. The normalized collisional energy (NCE) value for HCD was varied from 30 to 60% to evaluate the optimal conditions for the fragmentation of peptide backbones and glycoconjugates. Our results indicated that HCD with lower NCE values preferentially fragmented the sugar chains attached to the peptides to generate a ladder of neutral loss of monosaccharides, thereby enabling the putative glycan structure characterization. In addition, detection of the oxonium ions enabled unambiguous differentiation of glycopeptides from non-glycopeptides. In contrast, HCD with higher NCE values preferentially fragmented the peptide backbone and, thus, provided information needed for confident peptide identification. We evaluated the HCD approach with alternating NCE parameters for confident characterization of intact N- and O-linked glycopeptides in a single liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis. In addition, we applied a novel data analysis pipeline, so-called GlycoFinder, to form a basis for automated data analysis. Overall, 38 unique intact glycopeptides corresponding to eight glycosylation sites (six N-linked and two O-linked sites) were confidently identified from a standard protein mixture. This approach provided concurrent characterization of both the peptide and the glycan, thereby enabling comprehensive structural characterization of glycoproteins in a single LC-MS/MS analysis.

| S-EPMC5627992 | biostudies-literature

Mapping the O-glycoproteome using site-specific extraction of O-linked glycopeptides (EXoO).

Project description:Protein glycosylation is one of the most abundant post-translational modifications. However, detailed analysis of O-linked glycosylation, a major type of protein glycosylation, has been severely impeded by the scarcity of suitable methodologies. Here, a chemoenzymatic method is introduced for the site-specific extraction of O-linked glycopeptides (EXoO), which enabled the mapping of over 3,000 O-linked glycosylation sites and definition of their glycans on over 1,000 proteins in human kidney tissues, T cells, and serum. This large-scale localization of O-linked glycosylation sites demonstrated that EXoO is an effective method for defining the site-specific O-linked glycoproteome in different types of sample. Detailed structural analysis of the sites identified revealed conserved motifs and topological orientations facing extracellular space, the cell surface, the lumen of the Golgi, and the endoplasmic reticulum (ER). EXoO was also able to reveal significant differences in the O-linked glycoproteome of tumor and normal kidney tissues pointing to its broader use in clinical diagnostics and therapeutics.

| S-EPMC6243375 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

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