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Single-crystal-to-single-crystal synthesis of a pseudostarch via topochemical azide–alkyne cycloaddition polymerization† † Electronic supplementary information (ESI) available. CCDC 2038869 and 2038870. For ESI and crystallographic data in CIF or other electronic format see DOI: 10.1039/d1sc03727g

ABSTRACT: There is high demand for polysaccharide-mimics as enzyme-stable substitutes for polysaccharides for various applications. Circumventing the problems associated with the solution-phase synthesis of such polymers, we report here the synthesis of a crystalline polysaccharide-mimic by topochemical polymerization. By crystal engineering, we designed a topochemically reactive crystal of a glucose-mimicking monomer decorated with azide and alkyne units. In the crystal, the monomers arrange in head-to-tail fashion with their azide and alkyne groups in a ready-to-react antiparallel geometry, suitable for their topochemical azide–alkyne cycloaddition (TAAC) reaction. On heating the crystals, these pre-organized monomer molecules undergo regiospecific TAAC polymerization, yielding 1,4-triazolyl-linked pseudopolysaccharide (pseudostarch) in a single-crystal-to-single-crystal manner. This crystalline pseudostarch shows better thermal stability than its amorphous form and many natural polysaccharides. Prudent crystal engineering allows head-to-tail arrangement of inositol monomer molecules pre-organizing azide and alkyne units of adjacent monomers in a ready-to-react manner. On heating regiospecific SCSC polymerization yields a starch-like polymer.

SUBMITTER: Ravi A

PROVIDER: S-EPMC8442703 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature

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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.

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