ChemBioChem

Cover image for Vol. 18 Issue 12

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. Small molecule inhibitors of the tumor suppressor Fhit

    Andreas Marx, Sandra Lange, Stephan Hacker, Philipp Schmid and Martin Scheffner

    Accepted manuscript online: 23 JUN 2017 02:52AM EST | DOI: 10.1002/cbic.201700226

  2. Dendrimer-based signal amplification of click-labelled DNA in situ

    Nada Raddaoui, Samuele Stazzoni, Leonhard Möckl, Bastien Viverge, Florian Geiger, Hanna Engelke, Christoph Bräuchle and Thomas Carell

    Accepted manuscript online: 22 JUN 2017 09:45AM EST | DOI: 10.1002/cbic.201700209

  3. A Nonbactericidal Zinc-Complexing Ligand as a Biofilm Inhibitor: Structure-Guided Contrasting Effects on Staphylococcus aureus Biofilm

    Vidushi Kapoor, Rajanikant Rai, Durairaj Thiyagarajan, Sandipan Mukherjee, Prof. Gopal Das and Prof. Aiyagari Ramesh

    Version of Record online: 22 JUN 2017 | DOI: 10.1002/cbic.201700139

    Thumbnail image of graphical abstract

    Anti-biofilm agents: Different structural motifs in zinc-chelating ligands can influence their anti-biofilm potential. A nuanced understanding of the structure–function correlation of zinc-chelating ligands can serve as a design guideline for potent synthetic biofilm inhibitors.

  4. Covalent Protein Labeling by SpyTag–SpyCatcher in Fixed Cells for Super-Resolution Microscopy

    Dr. Veronica Pessino, Dr. Y. Rose Citron, Dr. Siyu Feng and Dr. Bo Huang

    Version of Record online: 22 JUN 2017 | DOI: 10.1002/cbic.201700177

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    I spy, with my little eye… We demonstrate the use of the covalent SpyTag–SpyCatcher system as a highly efficient epitope-like tag for fluorescent labeling of overexpressed, as well as endogenous, intracellular proteins in fixed cells for both conventional and super-resolution microscopy.

  5. Exploring the Structural Space of the Galectin-1–Ligand Interaction

    Dr. Nadja Bertleff-Zieschang, Julian Bechold, Dr. Clemens Grimm, Dr. Michael Reutlinger, Dr. Petra Schneider, Prof. Dr. Gisbert Schneider and Prof. Dr. Jürgen Seibel

    Version of Record online: 22 JUN 2017 | DOI: 10.1002/cbic.201700251

    Thumbnail image of graphical abstract

    In a bind: Expansion of the natural N-acetyllactosamine (LacNAc) binding scaffold by a synthetic multifunctional LacNAc mimetic leads to expanded ligands that share a binding mode that is almost identical to that of the natural carbohydrate template. X-ray crystallography provides a structural understanding of the galectin-1–ligand interactions. The results of this study enable the development of ligands for members of the galectin target family.

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