Cover image for Vol. 18 Issue 10

Editor: Meghan Campbell; Editorial Board Chairs: Thomas Carell, Donald Hilvert, Barbara Imperiali

Online ISSN: 1439-7633

Associated Title(s): ChemCatChem, ChemMedChem, ChemPhysChem, ChemSusChem

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May 04, 2017

Two recent VIP papers on mass spectrometry and mannosidase inhibitors

Very Important Paper: Mapping the Interactions of Selective Biochemical Probes of Antibody Conformation by Hydrogen--Deuterium Exchange Mass Spectrometry

Ulrike Leurs, Hermann Beck, Lea Bonnington, Ingo Lindner, Ewa Pol, Kasper Rand*

A major challenge during the development of therapeutic antibodies (IgG) is the assessment of changes to their higher-order structure. Now, K. Rand (University of Copenhagen, Denmark) and co-workers investigate the use of engineered Fab fragments, designed to bind to conserved regions of the IgG that are prone to undergo conformational changes. The selectivity of each probe to bind to distinct correctly folded parts of the IgG was identified by a combination of hydrogen--deuterium exchange mass spectrometry experiments (HDX-MS) and electron transfer dissociation (ETD). The use of these biochemical probes was also demonstrated in a surface plasmon resonance assay, which showed that their binding is sensitive to conformational changes occurring in IgG upon oxidation.

Very Important Paper: Selective Manipulation of Discrete Mannosidase Activities in the Endoplasmic Reticulum by Using Reciprocally Selective Inhibitors

Taiki Kuribara, Makoto Hirano, Gaetano Speciale, Spencer J. Williams, Yukishige Ito, Kiichiro Totani*

Around one third of N-linked glycoproteins produced in the cell fail to properly fold and must be detected and appropriately disposed of. Yet, the precise details of which glycan structures encode secretion and degradation signals are obscure. K. Totani (Seikei University, Japan) and co-workers report that known glycosidase inhibitors (deoxynojirimycin and deoxymannojirimycin) can selectively inhibit glycan-editing mannosidases provided their concentrations are carefully controlled. Using inhibitors to control the processing of a synthetic N-glycan in an ER-fraction, two discrete glycan processing pathways leading to secretion and degradation were discovered. This work provides fundamental insights into the signals that control the fate of glycoproteins.

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Recently Published Articles

  1. Targeting G-protein-coupled receptors by Capture Compound Mass Spectrometry (CCMS) - a case study with sertindole

    Christian Blex, Simon Michaelis, Anna K. Schrey, Jens Furkert, Jenny Eichhorst, Kathrin Bartho, Frederick G. Quast, Anett Marais, Matthias Hakelberg, Uschi Gruber, Sylvia Niquet, Oliver Popp, Friedrich Kroll, Michael Sefkow, Ralf Schülein, Dreger Mathias and Hubert Köster

    Accepted manuscript online: 29 MAY 2017 12:20PM EST | DOI: 10.1002/cbic.201700152

  2. Endo-α-Mannosidase-Catalyzed Transglycosylation

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    Version of Record online: 29 MAY 2017 | DOI: 10.1002/cbic.201700111

    Thumbnail image of graphical abstract

    Golgiendo-α-mannosidase (G-EM) as atrans-glycosylation catalyst: Transglycosylation mediated by glycoside hydrolases is valuable for the chemo-enzymatic synthesis of oligosaccharides. We developed a novel transglycosylation reaction mediated by a mutant of G-EM (E407D) with α-fluorinated glucosyl mannoside as a donor. This reaction was applied to the synthesis of a natural high-mannose-type dodecasaccharide.

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    Accepted manuscript online: 29 MAY 2017 06:25AM EST | DOI: 10.1002/cbic.201700053

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    Version of Record online: 26 MAY 2017 | DOI: 10.1002/cbic.201700204

    Thumbnail image of graphical abstract

    Reaching out and grabbing hold of specificity: Interstrand crosslinking chemistry can be used for highly selective covalent anchoring of a probe to a specific nucleic acid target sequence. We developed a new crosslinking reaction that uses probes prepared in a one-step procedure from inexpensive commercial reagents to achieve excellent sequence specificity under isothermal assay conditions.

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