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Surface modification of polymeric micelles by strain-promoted alkyne-azide cycloadditions.

ABSTRACT: Organomicelles modified by surface dibenzylcyclooctyne moieties can conveniently be functionalized by strain-promoted alkyne-azide cycloadditions. The ligation approach is highly efficient, does not require toxic reagents and is compatible with a wide variety of functional modules. Interactions of proteins with surface ligands of the micelles have been studied by AFM, which revealed that it leads to disassembly of the particles thereby providing a mechanism for triggered drug release.

SUBMITTER: Guo J

PROVIDER: S-EPMC3059085 | biostudies-literature | 2010 Dec

REPOSITORIES: biostudies-literature

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Surface modification of polymeric micelles by strain-promoted alkyne-azide cycloadditions.

Guo Jun J Chen Guojun G Ning Xinghai X Wolfert Margreet A MA Li Xiuru X Xu Bingqian B Boons Geert-Jan GJ

Chemistry (Weinheim an der Bergstrasse, Germany) 20101201 45

Organomicelles modified by surface dibenzylcyclooctyne moieties can conveniently be functionalized by strain-promoted alkyne-azide cycloadditions. The ligation approach is highly efficient, does not require toxic reagents and is compatible with a wide variety of functional modules. Interactions of proteins with surface ligands of the micelles have been studied by AFM, which revealed that it leads to disassembly of the particles thereby providing a mechanism for triggered drug release. ...[more]

PMID: 21077066

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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

Surface modification of polymeric micelles by strain-promoted alkyne-azide cycloadditions.

Publications

Surface modification of polymeric micelles by strain-promoted alkyne-azide cycloadditions.

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