ChemBioChem

Cover image for ChemBioChem

March 18, 2013

Volume 14, Issue 5

Pages 525–654

  1. Cover Pictures

    1. Top of page
    2. Cover Pictures
    3. Graphical Abstract
    4. News
    5. Review
    6. Communications
    7. Full Papers
    1. You have free access to this content
      Cover Picture: The Protein Corona Mediates the Impact of Nanomaterials and Slows Amyloid Beta Fibrillation (ChemBioChem 5/2013) (page 525)

      Prof. Morteza Mahmoudi, Marco P. Monopoli, Meisam Rezaei, Iseult Lynch, Filippo Bertoli, Dr. Jennifer J. McManus and Prof. Kenneth A. Dawson

      Article first published online: 11 MAR 2013 | DOI: 10.1002/cbic.201390012

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      The cover picture shows that the presence of the protein corona at the surface of nanomaterials inhibits the fibrillation process of amyloid beta (Aβ) monomers. Several different nanomaterials [i.e., silica (100 and 200 nm), polystyrene with carboxyl surface modification (100 nm), and multi-walled carbon nanotubes (10–40 nm in diameter and 0.1–10 mm in length)] were used, and their effects on the Aβ fibrillation process were probed in the absence and presence of a protein corona, as well as well as under conditions under whic the protein corona was denatured. In their communication on p. 568 ff., M. Mahmoudi, J. J. McManus, K. A. Dawson, et al. show that the protein corona creates a shell at the surface of nanomaterials, regardless of their physico-chemical properties (e.g., size, core composition, shape, and surface properties), that reduces the levels of Aβ fibril formation.

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      Inside Cover: The C-Terminal Extended Serine Residue Is Absolutely Required in Nosiheptide Maturation (ChemBioChem 5/2013) (page 526)

      Weiying Liu, Min Ma, Yanjiu Xue, Dr. Nan Liu, Dr. Shuzhen Wang and Prof. Dr. Yijun Chen

      Article first published online: 11 MAR 2013 | DOI: 10.1002/cbic.201390013

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      The inside cover picture shows the necessity of the extended Ser13 residue of the core peptide in the process of nosiheptide maturation; this residue cannot be replaced by other amino acids without loss of function. For more details, see the paper by S. Wang, Y. Chen, et al. on p. 573 ff.

  2. Graphical Abstract

    1. Top of page
    2. Cover Pictures
    3. Graphical Abstract
    4. News
    5. Review
    6. Communications
    7. Full Papers
    1. Graphical Abstract: ChemBioChem 5/2013 (pages 527–532)

      Article first published online: 11 MAR 2013 | DOI: 10.1002/cbic.201390014

  3. News

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    3. Graphical Abstract
    4. News
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    1. Spotlights on our sister journals: ChemBioChem 5/2013 (pages 536–538)

      Article first published online: 11 MAR 2013 | DOI: 10.1002/cbic.201390015

  4. Review

    1. Top of page
    2. Cover Pictures
    3. Graphical Abstract
    4. News
    5. Review
    6. Communications
    7. Full Papers
    1. You have free access to this content
      Fluorescent Probes for G-Quadruplex Structures (pages 540–558)

      Balayeshwanth R. Vummidi, Dr. Jawad Alzeer and Prof. Dr. Nathan W. Luedtke

      Article first published online: 25 FEB 2013 | DOI: 10.1002/cbic.201200612

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      Positive discrimination: We present the key photophysical, biophysical, and biological properties of small molecules and modified oligonucleotides developed for discriminating G-quadruplex structures from other nucleic acids by fluorescence. The major challenges facing the development of fluorescent probes for cellular G-quadruplexes are presented.

  5. Communications

    1. Top of page
    2. Cover Pictures
    3. Graphical Abstract
    4. News
    5. Review
    6. Communications
    7. Full Papers
    1. Peptide Ligation–Desulfurization Chemistry at Arginine (pages 559–563)

      Lara R. Malins, Dr. Katie M. Cergol and Assoc. Prof. Richard J. Payne

      Article first published online: 20 FEB 2013 | DOI: 10.1002/cbic.201300049

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      The utility of a new β-thiol arginine building block in ligation–desulfurization chemistry has been demonstrated through reactions and kinetic studies with a range of peptide thioesters. Application of the method is highlighted by a one-pot, kinetically controlled, rapid ligation to generate a 7 kDa MUC1 glycopeptide.

    2. You have full text access to this OnlineOpen article
      An Enzymatic Route to Selenazolines (pages 564–567)

      Dr. Jesko Koehnke, Falk Morawitz, Andrew F. Bent, Dr. Wael E. Houssen, Dr. Sally L. Shirran, Dr. Matthew A. Fuszard, Dr. Iain A. Smellie, Dr. Catherine H. Botting, Prof. Margaret C. M. Smith, Prof. Marcel Jaspars and Prof. James H. Naismith

      Article first published online: 18 FEB 2013 | DOI: 10.1002/cbic.201300037

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      Ringing the changes: Selenazolines have applications in medicinal chemistry, but their synthesis is challenging. We report a new convenient and less toxic route to these heterocycles that starts from commercially available selenocysteine. The new route depends on a heterocyclase enzyme that creates oxazolines and thiazolines from serines/threonines and cysteines.

    3. The Protein Corona Mediates the Impact of Nanomaterials and Slows Amyloid Beta Fibrillation (pages 568–572)

      Prof. Morteza Mahmoudi, Marco P. Monopoli, Meisam Rezaei, Iseult Lynch, Filippo Bertoli, Dr. Jennifer J. McManus and Prof. Kenneth A. Dawson

      Article first published online: 18 FEB 2013 | DOI: 10.1002/cbic.201300007

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      Put your coat on: It is well recognized that the surfaces of nanomaterials in biological media are covered by various biomolecules (e.g., proteins). A) The protein corona creates a shell over different nanomaterials, regardless of their physicochemical properties (e.g., composition and shape), resulting in reduced levels of amyloid beta fibril formation. B) Pristine nanomaterials might have acceleratory effects on the fibrillation of amyloid beta.

    4. The C-Terminal Extended Serine Residue Is Absolutely Required in Nosiheptide Maturation (pages 573–576)

      Weiying Liu, Min Ma, Yanjiu Xue, Dr. Nan Liu, Dr. Shuzhen Wang and Prof. Dr. Yijun Chen

      Article first published online: 25 FEB 2013 | DOI: 10.1002/cbic.201200681

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      Serine qua non: Substitution of the extended Ser13 in the core peptide of nosiheptide by analogous amino acids prevented enamide dealkylation of the terminal residue for nosiheptide maturation.

    5. Dissecting the Roles of the N- and C-Flanking Residues of Acetyllysine Substrates for SIRT1 Activity (pages 577–581)

      Roman Meledin, Prof. Ashraf Brik and Prof. Amir Aharoni

      Article first published online: 20 FEB 2013 | DOI: 10.1002/cbic.201200727

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      SIRT1 specificity: The multispecific SIRT1 enzyme catalyzes the deacetylation of acetyllysine residues within protein targets. However, little is known regarding the molecular basis for SIRT1 substrate recognition. Kinetic analysis of SIRT1 with a panel of peptide substrates shows the high importance of the region N-flanking the target acetyllysine and its high conservation through evolution.

  6. Full Papers

    1. Top of page
    2. Cover Pictures
    3. Graphical Abstract
    4. News
    5. Review
    6. Communications
    7. Full Papers
    1. Carnosine Inhibits Aβ42 Aggregation by Perturbing the H-Bond Network in and around the Central Hydrophobic Cluster (pages 583–592)

      Dr. Francesco Attanasio, Dr. Marino Convertino, Dr. Andrea Magno, Prof. Amedeo Caflisch, Dr. Alessandra Corazza, Dr. Haritha Haridas, Prof. Gennaro Esposito, Dr. Sebastiano Cataldo, Prof. Bruno Pignataro, Dr. Danilo Milardi and Prof. Enrico Rizzarelli

      Article first published online: 25 FEB 2013 | DOI: 10.1002/cbic.201200704

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      Dropping your H's/Ban the bond: Inspired by the body of evidence for a neuroprotective activity of carnosine, we investigated whether this dipeptide hinders Aβ42 growth in vitro. Our results indicate that despite the inability of carnosine to form stable contacts with Aβ, it might block aggregation by perturbing the propensity of the peptide to form H-bonds.

    2. Readily Accessible Fluorescent Probes for Sensitive Biological Imaging of Hydrogen Peroxide (pages 593–598)

      Kevin B. Daniel, Arpita Agrawal, Prof. Dr. Marianne Manchester and Prof. Dr. Seth M. Cohen

      Article first published online: 21 FEB 2013 | DOI: 10.1002/cbic.201200724

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      Turning on the light: The preparation, reactivity, and imaging properties of a new class of fluorescence-based molecular probes is reported for the detection of endogenous hydrogen peroxide (H2O2). These probes are easy to synthesize, which should make them an accessible tool for probing the chemical biology of reactive oxygen species.

    3. The Interaction of Isopenicillin N Synthase with Homologated Substrate Analogues δ-(L-α-Aminoadipoyl)-L-homocysteinyl-D-Xaa Characterised by Protein Crystallography (pages 599–606)

      Dr. Adam Daruzzaman, Dr. Ian J. Clifton, Dr. Robert M. Adlington, Prof. Sir Jack E. Baldwin and Dr. Peter J. Rutledge

      Article first published online: 6 MAR 2013 | DOI: 10.1002/cbic.201200728

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      Loose fit: IPNS catalyses the central step in penicillin biosynthesis. Substrate analogues containing L-homocysteine in place of the natural substrate's L-cysteine residue are not converted into bicyclic products. Crystal structures for IPNS complexes with two such analogues reveal that the additional CH2 unit affords considerable conformational freedom when these analogues bind to IPNS.

    4. You have full text access to this OnlineOpen article
      Luminescent Conjugated Oligothiophenes for Sensitive Fluorescent Assignment of Protein Inclusion Bodies (pages 607–616)

      Therése Klingstedt, Dr. Cristiane Blechschmidt, Dr. Anna Nogalska, Dr. Stefan Prokop, Bo Häggqvist, Dr. Olof Danielsson, Prof. W. King Engel, Prof. Valerie Askanas, Prof. Frank L. Heppner and Dr. K. Peter R. Nilsson

      Article first published online: 28 FEB 2013 | DOI: 10.1002/cbic.201200731

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      Bright bodies! The unique optical properties of luminescent conjugated oligothiophenes have been utilized in fluorescent probes for rapid and accurate detection and spectral assignment of protein inclusion bodies in sporadic inclusion-body myositis.

    5. Cyclization of the Antimicrobial Peptide Gomesin with Native Chemical Ligation: Influences on Stability and Bioactivity (pages 617–624)

      Dr. Lai Yue Chan, Veronica M. Zhang, Dr. Yen-hua Huang, Dr. Norman C. Waters, Dr. Paramjit S. Bansal, Prof. David J. Craik and Prof. Norelle L. Daly

      Article first published online: 20 FEB 2013 | DOI: 10.1002/cbic.201300034

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      Going round in cycles: The use of native chemical ligation to link the N and C termini of gomesin with a one-residue linker is reported. These findings support the generalization of the concept of using backbone cyclization to enhance the therapeutic potential of peptides.

    6. Alanine Scan of the Peptide Antibiotic Feglymycin: Assessment of Amino Acid Side Chains Contributing to Antimicrobial Activity (pages 625–632)

      Dr. Anne Hänchen, Dr. Saskia Rausch, Benjamin Landmann, Dr. Luigi Toti, Antje Nusser and Prof. Dr. Roderich D. Süssmuth

      Article first published online: 27 FEB 2013 | DOI: 10.1002/cbic.201300032

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      À la mode scanning: An alanine scan of the peptide antibiotic feglymycin was performed by solution-phase peptide synthesis to assess the significance of individual amino acid side chains for its biological activity. Antibacterial activity against Staphylococcus aureus and the inhibition of enzymes MurA and MurC depend on different amino acids.

    7. Structure and Biosynthesis of Fimsbactins A–F, Siderophores from Acinetobacter baumannii and Acinetobacter baylyi (pages 633–638)

      Anna Proschak, Patrice Lubuta, Peter Grün, Dr. Frank Löhr, Dr. Gottfried Wilharm, Veronique De Berardinis and Prof. Dr. Helge B. Bode

      Article first published online: 1 MAR 2013 | DOI: 10.1002/cbic.201200764

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      There can be more than one: The structure and biosynthesis of a novel class of siderophores, with fimsbactin A as the main compound, has been identified in different Acinetobacter strains, including different pathogenic Acinetobacter baumannii strains.

    8. Improved Conformational Stability of the Visual G Protein-Coupled Receptor Rhodopsin by Specific Interaction with Docosahexaenoic Acid Phospholipid (pages 639–644)

      Dr. Maria Jesús Sánchez-Martín, Dr. Eva Ramon, Prof. Juan Torrent-Burgués and Prof. Pere Garriga

      Article first published online: 27 FEB 2013 | DOI: 10.1002/cbic.201200687

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      Rhodopsin stability is improved in docosahexaenoic acid (DHA) liposomes by specific DHA–rhodopsin interaction. Correctly folded opsin conformation is preserved by the phospholipid environment, thus allowing in vitro chromophore regeneration of immunopurified receptor long after photobleaching.

    9. Spectroscopic and Theoretical Study on Electronically Modified Chromophores in LOV Domains: 8-Bromo- and 8-Trifluoromethyl-Substituted Flavins (pages 645–654)

      Dr. Madina Mansurova, Julian Simon, Dr. Susanne Salzmann, Prof. Dr. Christel M. Marian and Prof. Dr. Wolfgang Gärtner

      Article first published online: 1 MAR 2013 | DOI: 10.1002/cbic.201200670

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      Vision in blue: Flavin derivatives, substituted at position 8 (R=bromo-, trifluoromethyl-) were synthesized and incorporated as chromophores into the blue-light-sensing LOV domain of YtvA from Bacillus subtilis. The resultant strong change in electronegativity significantly modifies the electronic and functional properties of the reconstituted LOV domains.

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