ChemBioChem

Cover image for Vol. 8 Issue 9

June 18, 2007

Volume 8, Issue 9

Pages 961–1078

  1. Cover Picture

    1. Top of page
    2. Cover Picture
    3. Graphical Abstract
    4. News
    5. Minireview
    6. Highlight
    7. Communications
    8. Full Papers
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    1. Cover Picture: Embedding the Amyloid β-Peptide Sequence in Green Fluorescent Protein Inhibits Aβ Oligomerization (ChemBioChem 9/2007) (page 961)

      Tsuyoshi Takahashi, Kenichi Ohta and Hisakazu Mihara

      Version of Record online: 1 JUN 2007 | DOI: 10.1002/cbic.200790026

      The cover picture shows a green fluorescent protein (GFP) variant in which an amyloid β-peptide (Aβ) sequence is embedded. Through self recognition Aβ can aggregate to toxic species such as soluble oligomers that form β-sheet structures, and this oligomerization is closely related to Alzheimer's disease (AD). Embedding the Aβ sequence in a GFP scaffold that contains stable β-sheet structures generates a pseudo-Aβ surface on GFP. Thus, the GFP variant can bind to Aβ with high affinity, and their interaction effectively inhibits Aβ oligomerization. This strategy could be applied to other amyloid-related diseases such as prion and Parkinson's diseases. For more information see the full paper by T. Takahashi et al. on p. 985 ff.

  2. Graphical Abstract

    1. Top of page
    2. Cover Picture
    3. Graphical Abstract
    4. News
    5. Minireview
    6. Highlight
    7. Communications
    8. Full Papers
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  3. News

    1. Top of page
    2. Cover Picture
    3. Graphical Abstract
    4. News
    5. Minireview
    6. Highlight
    7. Communications
    8. Full Papers
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  4. Minireview

    1. Top of page
    2. Cover Picture
    3. Graphical Abstract
    4. News
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    7. Communications
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    1. Biosynthesis of Nitro Compounds (pages 973–977)

      Robert Winkler and Christian Hertweck

      Version of Record online: 4 MAY 2007 | DOI: 10.1002/cbic.200700042

      Thumbnail image of graphical abstract

      Green nitro. While many nitrated natural products from a variety of sources have been isolated, their biosynthetic origin is less well understood. Two routes can lead to these highly energetic natural products: biological aryl nitration and highly selective enzymatic N-oxidation. Despite the numerous nitrated natural products, only a few of the enzymes involved in nitro group formation have been identified, and only recently have mechanistic studies provided insight into these reactions.

  5. Highlight

    1. Top of page
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    3. Graphical Abstract
    4. News
    5. Minireview
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    1. Reactivity Recognition by TRPA1 Channels (pages 979–980)

      Menekse Cebi and Ulrich Koert

      Version of Record online: 10 MAY 2007 | DOI: 10.1002/cbic.200700113

      Thumbnail image of graphical abstract

      Taste the seasoning. Sensing of the pungent principles of mustard and horseradish is caused by a covalent protein modification that activates the ion-channel receptor involved rather than a direct lock-and-key mechanism.

  6. Communications

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    2. Cover Picture
    3. Graphical Abstract
    4. News
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    1. Straightforward Preparation and Assay of Aspartyl Protease Substrates with an Internal Thioester Linkage (pages 981–984)

      Yazmín T. Rosa-Bauzá, Frederic Berst and Jonathan A. Ellman

      Version of Record online: 10 MAY 2007 | DOI: 10.1002/cbic.200700008

      Thumbnail image of graphical abstract

      Preparation and continuous assay. The solid-phase synthesis of peptide substrates that contain a scissile thioester bond is described. In addition, as demonstrated for cathepsin D, the first use of thioester substrates for the continuous monitoring of aspartyl protease activity is reported.

    2. Embedding the Amyloid β-Peptide Sequence in Green Fluorescent Protein Inhibits Aβ Oligomerization (pages 985–988)

      Tsuyoshi Takahashi, Kenichi Ohta and Hisakazu Mihara

      Version of Record online: 14 MAY 2007 | DOI: 10.1002/cbic.200700108

      Thumbnail image of graphical abstract

      Against a green background. We have embedded the amyloid β-peptide (Aβ) sequence into the green fluorescent protein (GFP) structure to generate a pseudo-Aβ surface on the β-barrel (see figure); this construct was highly active in inhibiting Aβ oligomerization. One GFP variant (P13H), which mimicked the parallel β sheets of Aβ, was found to bind Aβ with high affinity and inhibit Aβ oligomerization, even though the concentration of P13H was lower than that of Aβ.

    3. Isolation of Peptides that Can Recognize Syndiotactic Polystyrene (pages 989–993)

      Takeshi Serizawa, Prapatsorn Techawanitchai and Hisao Matsuno

      Version of Record online: 10 MAY 2007 | DOI: 10.1002/cbic.200700133

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      Two different types of peptide with high specificity for sPS. Phage libraries of random heptamer peptides were applied to syndiotactic polystyrene (sPS) film surfaces. Enzyme-linked immunosorbent assays with phage clones and a library quantitatively revealed greater apparent binding constants of clones to the target polystyrene than to atactic and isotactic polystyrenes. The clones also recognized the presence or absence of complexed solvents in the target films.

    4. Membrane Protein Stoichiometry Determined from the Step-Wise Photobleaching of Dye-Labelled Subunits (pages 994–999)

      Somes K. Das, Manjula Darshi, Stephen Cheley, Mark I. Wallace and Hagan Bayley

      Version of Record online: 14 MAY 2007 | DOI: 10.1002/cbic.200600474

      Thumbnail image of graphical abstract

      Body count.In a generally applicable approach, the number of subunits in fluorescently-labelled protein complexes has been determined by counting photobleaching steps from individual molecules (see figure). The distribution of steps in the pore-forming toxins α-haemolysin and leukocidin indicate seven subunits for α-hemolysin, and four LukF and four LukS subunits for leukocidin.

  7. Full Papers

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    1. The Cyclotide Fingerprint in Oldenlandia affinis: Elucidation of Chemically Modified, Linear and Novel Macrocyclic Peptides (pages 1001–1011)

      Manuel Rey R. Plan, Ulf Göransson , Richard J. Clark, Norelle L. Daly, Michelle L. Colgrave and David J. Craik

      Version of Record online: 30 MAY 2007 | DOI: 10.1002/cbic.200700097

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      All tied up! This study describes the discovery and biochemical characterisation of a suite of novel circular and cystine-knotted plant proteins, known as cyclotides, which have a range of pharmacological properties. In addition, this is the first report on potential degradation pathways of cyclotides, and the findings are thus valuable for potential uses of these molecules in pharmaceutical and agricultural applications.

    2. Correctors of Protein Trafficking Defects Identified by a Novel High-Throughput Screening Assay (pages 1012–1020)

      Graeme W. Carlile , Renaud Robert , Donglei Zhang, Katrina A. Teske, Yishan Luo, John W. Hanrahan and David Y. Thomas

      Version of Record online: 11 MAY 2007 | DOI: 10.1002/cbic.200700027

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      Helping lost proteins find the correct home. These are two of several compounds identified as hits in a novel high-throughput correction assay. The compounds assist a misfolded version of the cystic fibrosis transmembrane conductance regulator protein to traffic to its correct destination. This assay works on the principle of using a tagged version of the mutant protein in a cell-based system, and monitors by immunofluorescence its arrival at the target location.

    3. Avidin Decorated Core–Shell Nanoparticles for Biorecognition Studies by Elastic Light Scattering (pages 1021–1028)

      Davide Prosperi, Carlo Morasso, Paolo Tortora, Diego Monti and Tommaso Bellini

      Version of Record online: 14 MAY 2007 | DOI: 10.1002/cbic.200600542

      Thumbnail image of graphical abstract

      Invisible sensors! Elastic light scattering enables the quantitative determination of protein–ligand binding that occurs at the surface of suitably designed nanoparticles with a core–shell morphology. The core material is an index-matched perfluoropolymer, which has been surface-functionalized with a few native avidin molecules embedded in an oligo(ethylene glycol) amphiphile monolayer. The resulting nanosensor was used to detect protein–ligand and protein–antibody interactions.

    4. A Fluorogenic Peptide Containing the Processing Site of Human SARS Corona Virus S-Protein: Kinetic Evaluation and NMR Structure Elucidation (pages 1029–1037)

      Ajoy Basak, Abhijit Mitra, Sarmistha Basak, Carolyn Pasko, Michel Chrétien and Pamela Seaton

      Version of Record online: 30 APR 2007 | DOI: 10.1002/cbic.200700007

      Thumbnail image of graphical abstract

      Cut and fuse. A key event in SARS infection is the proteolytic cleavage of viral spike protein by host proteases. By using intramolecularly quenched fluorogenic (IQF) peptides based on hSARS-CoV spike protein and in vitro studies, we show that in addition to furin, proprotein convertases PC5 and PC7 cleave the model IQF peptide. Cleavage could be blocked by the PC inhibitor, α1-PDX, in a dose-dependent manner. The 3D structure of the model peptide was investigated by circular dichromism and 2D 1H NMR spectroscopy.

    5. Penetration of the Antimicrobial Peptide Dicynthaurin into Phospholipid Monolayers at the Liquid–Air Interface (pages 1038–1047)

      Frank Bringezu, Monika Majerowicz, Elena Maltseva, Shaoying Wen, Gerald Brezesinski and Alan J. Waring

      Version of Record online: 10 MAY 2007 | DOI: 10.1002/cbic.200600503

      Thumbnail image of graphical abstract

      Losing your integrity. Dicynthaurin, an antimicrobial peptide derived from the tunicate Halocynthia auranthium, exhibits a remarkably broad-spectrum activity against several microorganisms. As membrane targeting is crucial for this activity, we present the first study of membrane–dicynthaurin interaction by using a biophysical approach. The results suggest that dicynthaurin is able to adsorb to the phosphatidylglycerol-rich inner cytoplasmic membrane of bacteria (see figure) and thus alters membrane integrity.

    6. Functional Characterization of the Recombinant N-Methyltransferase Domain from the Multienzyme Enniatin Synthetase (pages 1048–1054)

      Till Hornbogen, Sean-Patrick Riechers, Bianka Prinz, Jeffrey Schultchen, Christine Lang, Sebastian Schmidt, Clemens Mügge, Suada Turkanovic, Roderich D. Süssmuth, Eva Tauberger and Rainer Zocher

      Version of Record online: 30 APR 2007 | DOI: 10.1002/cbic.200700076

      Thumbnail image of graphical abstract

      The heart of the matter: The N-methyltransferase domain of enniatin synthetase (ENMT) from Fusarium scirpi was functionally expressed. The recombinant protein was found to be active by using S-adenosyl methionine (AdoMet) as methyl donor in cross-linking experiments and saturation transfer difference NMR spectroscopy studies (see scheme). Methyl group transfer was demonstrated by using aminoacyl-N-acetylcysteamine thioesters as substrates.

    7. A Mass Spectrometric Investigation of Native and Oxidatively Inactivated Chloroperoxidase (pages 1055–1062)

      Carl Elovson Grey, Martin Hedström and Patrick Adlercreutz

      Version of Record online: 10 MAY 2007 | DOI: 10.1002/cbic.200700091

      Thumbnail image of graphical abstract

      Chop and change. Chloroperoxidase (CPO) was found to be inactivated when it was used to catalyze the oxidation of indole with H2O2. Two observations were made by using mass spectrometry that could explain the enzyme inactivation. First, Cys50, which is an essential amino acid due to its function as the axial ligand to the iron in the heme, was found to be oxidized (see scheme). Secondly, the signal from the heme disappeared.

    8. An Activity, Stability and Selectivity Comparison of Propioin Synthesis by Thiamine Diphosphate-Dependent Enzymes in a Solid/Gas Bioreactor (pages 1063–1070)

      Renaud Mikolajek, Antje C. Spiess, Martina Pohl, Sylvain Lamare and Jochen Büchs

      Version of Record online: 11 MAY 2007 | DOI: 10.1002/cbic.200700095

      Thumbnail image of graphical abstract

      Stuck on a hard place. Benzaldehyde lyase and benzoylformate decarboxylase catalyze the ligation of two propanal molecules to propioin (see figure). These enzymes were immobilized on a porous support and investigated in a solid/gas bioreactor. Experimental differences between both enzymes were observed in term of enzymatic activity, biocatalyst stability and product enantioselectivity.

    9. Specifically Immobilised Aldo/Keto Reductase AKR1A1 Shows a Dramatic Increase in Activity Relative to the Randomly Immobilised Enzyme (pages 1071–1076)

      Kai Holland-Nell and Annette G. Beck-Sickinger

      Version of Record online: 16 MAY 2007 | DOI: 10.1002/cbic.200700056

      Thumbnail image of graphical abstract

      A much more active surface-bound enzyme than any obtained by adsorptive or unspecific immobilisation. The aldo/keto reductase AKR1A1 was selectively biotinylated by expressed protein ligation and site-specifically immobilised on streptavidin templates. In contrast to enzyme immobilised by random immobilisation methods, the enzyme fully maintained its biological activity.

  8. Preview

    1. Top of page
    2. Cover Picture
    3. Graphical Abstract
    4. News
    5. Minireview
    6. Highlight
    7. Communications
    8. Full Papers
    9. Preview
    1. Preview: ChemBioChem 10/2007 (page 1078)

      Version of Record online: 1 JUN 2007 | DOI: 10.1002/cbic.200790025

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