Dataset Information

Polymer immobilized Cu(I) formation and azide-alkyne cycloaddition: A one pot reaction.

ABSTRACT: During the polymerization of aniline using copper sulphate, act as an oxidizing agent, the in-situ synthesized Cu(I) ion catalyzed the cyclo-addition between azides and alkynes. This work represents the merging of two steps, synthesis of the catalyst and application of the catalyst, in a one pot reaction. The elimination of the separate catalyst synthesis step is economic in terms of cost and time. As aniline was used as one of the reactant components so there is no requirement to use additional base for this reaction that further eliminates the cost of the process. Again, the catalyst can be readily recovered by filtration and efficiently used for the several sets of reactions without any significant loss of catalytic activity.

SUBMITTER: Islam RU

PROVIDER: S-EPMC4603298 | biostudies-literature | 2015 May

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Polymer immobilized Cu(I) formation and azide-alkyne cycloaddition: A one pot reaction.

Islam Rafique Ul RU Taher Abu A Choudhary Meenakshi M Siwal Samarjeet S Mallick Kaushik K

Scientific reports 20150512

During the polymerization of aniline using copper sulphate, act as an oxidizing agent, the in-situ synthesized Cu(I) ion catalyzed the cyclo-addition between azides and alkynes. This work represents the merging of two steps, synthesis of the catalyst and application of the catalyst, in a one pot reaction. The elimination of the separate catalyst synthesis step is economic in terms of cost and time. As aniline was used as one of the reactant components so there is no requirement to use additional ...[more]

PMID: 25966018

Similar Datasets

Project description:O-linked β-N-acetylglucosamine (O-GlcNAc) is emerging as an essential protein post-translational modification in a range of organisms. It is involved in various cellular processes such as nutrient sensing, protein degradation, gene expression, and is associated with many human diseases. Despite its importance, identifying O-GlcNAcylated proteins is a major challenge in proteomics. Here, using peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz) as a bioorthogonal chemical handle, we described a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells. In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne. After conjugation with click chemistry in vitro and enrichment via streptavidin resin, proteins with O-GlcNAc modification were separated by SDS-PAGE and identified with mass spectrometry. Proteomics data analysis revealed that 229 putative O-GlcNAc modified proteins were identified with Biotin-Diazo-Alkyne conjugated sample and 188 proteins with Biotin-DIBO-Alkyne conjugated sample, among which 114 proteins were overlapping. Interestingly, 74 proteins identified from Biotin-Diazo-Alkyne conjugates and 46 verified proteins from Biotin-DIBO-Alkyne conjugates could be found in the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html). These results suggested that CuAAC with Biotin-Diazo-Alkyne represented a more powerful method in proteomics with higher protein identification and better accuracy compared to SPAAC. The proteomics credibility was also confirmed by the molecular function and cell component gene ontology (GO). Together, the method we reported here combining metabolic labeling, click chemistry, affinity-based enrichment, SDS-PAGE separation, and mass spectrometry, would be adaptable for other post-translationally modified proteins in proteomics.

Dataset Information

Polymer immobilized Cu(I) formation and azide-alkyne cycloaddition: A one pot reaction.

Publications

Polymer immobilized Cu(I) formation and azide-alkyne cycloaddition: A one pot reaction.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets