ChemBioChem

Cover image for Vol. 15 Issue 18

Editor: Peter Gölitz; Editorial Board Chairs: Thomas Carell, Donald Hilvert, Barbara Imperiali

Online ISSN: 1439-7633

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

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December 04, 2014

Very Important Paper: Reconstructing the Discontinuous and Conformational β1/β3-Loop Binding Site on hFSH/hCG by Using Highly Constrained Multicyclic Peptides

Linde E.J. Smeenk, Drohpatie Timmers-Parohi, Joris J. Benschop, Wouter C. Pouijk, Henk Hiemstra, Jan H. van Maarseveen, Peter Timmerman*

Mimicking the binding surface of a protein with peptide-based “small molecules” remains a key challenge in biomedical sciences. In order to achieve maximal binding, different peptide domains involved in binding need to be properly linked and positioned onto a core scaffold molecule. Now, Peter Timmerman (University of Amsterdam) and co-workers describe a novel methodology for producing peptide-based mimics of discontinuous epitopes on hFSHβ and hCGβ. They show the need for multiple constraints for successful mimicry of these complex epitopes. Moreover, tri- and tetracyclic peptides show an over 100-fold improvement in binding, when compared to linear and single-loop peptides. These newly developed mimics may eventually provide novel therapeutics or ultimately be used as synthetic vaccines.

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    Hen Egg-White Lysozyme Crystallisation: Protein Stacking and Structure Stability Enhanced by a Tellurium(VI)-Centred Polyoxotungstate

    Aleksandar Bijelic, Christian Molitor, Dr. Stephan G. Mauracher, Dr. Rami Al-Oweini, Prof. Dr. Ulrich Kortz and Annette Rompel

    Article first published online: 17 DEC 2014 | DOI: 10.1002/cbic.201402597

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    Polyoxometalate-mediated protein crystallisation: An Anderson–Evans-type polyoxometalate, Na6[TeW6O24]22 H2O (TEW), has been applied as crystallisation additive for the crystallisation of hen egg-white lysozyme. X-ray structure analysis revealed the active involvement of TEW in the protein crystal packing inducing a new crystal form. TEW is able to crosslink single protein monomers electrostatically and thus facilitate protein crystallisation.

  2. Achieving Single-Nucleotide Resolution of 5-Methylcytosine Detection with TALEs

    Grzegorz Kubik and Dr. Daniel Summerer

    Article first published online: 17 DEC 2014 | DOI: 10.1002/cbic.201402408

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    Engineered transcription-activator-like effectors (TALEs) are the first DNA-binding molecules to provide single-nucleotide resolution of 5-methylcytosine (mC) detection with fully programmable sequence selectivity. A single cytosine (C) in a DNA sequence is selectively interrogated for its mC-modification level by targeting it with a discriminatory TALE repeat.

  3. Applying γ-Substituted Prolines in the Foldon Peptide: Polarity Contradicts Preorganization

    Dennis Dietz, Dr. Vladimir Kubyshkin and Prof. Dr. Nediljko Budisa

    Article first published online: 16 DEC 2014 | DOI: 10.1002/cbic.201402654

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    Tailoring the properties of the­ foldon­ structure: γ-Substituted proline units were successfully applied to the engineering of the foldon trimerization tag. The initial structure was found to be largely unaltered but the melting temperatures were found to be substantially affected, allowing both stabilization and destabilization of the native fold.

  4. Genome Mining-Directed Activation of a Silent Angucycline Biosynthetic Gene Cluster in Streptomyces chattanoogensis

    Dr. Zhenxing Zhou, Qingqing Xu, Dr. Qingting Bu, Dr. Yuanyang Guo, Dr. Shuiping Liu, Yu Liu, Dr. Yiling Du and Prof. Yongquan Li

    Article first published online: 15 DEC 2014 | DOI: 10.1002/cbic.201402577

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    No longer hidden: Overexpression of a pathway-specific regulator gene under the constitutive ermE* promoter led to activation of a cryptic angucycline biosynthetic gene cluster. Two novel members of the angucycline family of antibiotics were isolated and elucidated.

  5. Characterization of the Gene Cluster CYP264B1-geoA from Sorangium cellulosum So ce56: Biosynthesis of (+)-Eremophilene and Its Hydroxylation

    Alexander Schifrin, Dr. Thuy T. B. Ly, Dr. Nils Günnewich, Dr. Josef Zapp, Dr. Verena Thiel, Prof. Dr. Stefan Schulz, Dr. Frank Hannemann, Dr. Yogan Khatri and Prof. Dr. Rita Bernhardt

    Article first published online: 12 DEC 2014 | DOI: 10.1002/cbic.201402443

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    Terpene synthases (TSs) and cytochromes P450 are key enzymes in biosynthesis pathways of terpenoids. We report the functional characterization of the gene cluster geoA-CYP264B1 from S. cellulosum So ce56. The TS forms the previously unknown sesquiterpene enantiomer (+)-eremophilene, the physiological substrate of the cytochrome P450. The sesquiterpene hydroxylase CYP264B1 conducts multiple hydroxylations on (+)-eremophilene.

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