Cover image for Vol. 10 Issue 9

Editor-in-Chief: Natalia Ortúzar

Impact Factor: 2.968

ISI Journal Citation Reports © Ranking: 2014: 19/59 (Chemistry Medicinal); 83/254 (Pharmacology & Pharmacy)

Online ISSN: 1860-7187

Associated Title(s): Angewandte Chemie International Edition, Chemistry - A European Journal, Chemistry – An Asian Journal, ChemBioChem, Medicinal Research Reviews, Molecular Informatics

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August 28, 2015

VIP: Acyclic Nucleoside Phosphonates as Plasmodium and Human HG(X)PRT Inhibitors

VIP: Acyclic Nucleoside Phosphonates as Plasmodium and Human HG(X)PRT InhibitorsGiven the development of resistance to current antimalarial medications, new treatments with novel modes of action are urgently needed to combat this infectious disease. Acyclic nucleoside phosphonates have been shown to be potent inhibitors of Plasmodium hypoxanthine-guanine-(xanthine) phosphoribosyltransferase [HG(X)PRT], a key enzyme of the parasitic purine nucleotide salvage pathway. Read more...

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  1. Synthesis and Evaluation of Novel Acyclic Nucleoside Phosphonates as Inhibitors of Plasmodium falciparum and Human 6-Oxopurine Phosphoribosyltransferases

    Dr. Martin M. Kaiser, Dr. Dana Hocková, Tzu-Hsuan Wang, Dr. Martin Dračínský, Dr. Lenka Poštová-Slavětínská, Eliška Procházková, Dr. Michael D. Edstein, Dr. Marina Chavchich, Dr. Dianne T. Keough, Dr. Luke W. Guddat and Dr. Zlatko Janeba

    Article first published online: 25 AUG 2015 | DOI: 10.1002/cmdc.201500322

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    Combating malaria: An efficient inhibition of plasmodial 6-oxopurine phosphoribosyltransferase, a key enzyme of the parasitic purine nucleotide salvage pathway, is a promising way to combat malaria. Novel acyclic nucleoside phosphonates were designed as potent inhibitors of phosphoribosyltransferases, and the mode of their binding in the enzyme active site was studied in detail.

  2. A Bisbenzamidine Phosphonate as a Janus-faced Inhibitor for Trypsin-like Serine Proteases

    Daniela Häußler, Tamara Scheidt, Dr. Marit Stirnberg, Prof. Dr. Torsten Steinmetzer and Prof. Dr. Michael Gütschow

    Article first published online: 25 AUG 2015 | DOI: 10.1002/cmdc.201500319

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    Two fragments, two modes: We designed a Janus-faced serine protease inhibitor by merging two benzamidine fragments, which impart the molecule with either irreversible or reversible inhibitory activity. Unexpected differences in potency toward trypsin-like proteases were found; the compound exhibits remarkable inhibitory activity against human thrombin. This hybrid approach is a useful way to obtain potent and selective inhibitors.

  3. (−)-Tarchonanthuslactone: Design of New Analogues, Evaluation of their Antiproliferative Activity on Cancer Cell Lines, and Preliminary Mechanistic Studies

    Luiz Fernando Toneto Novaes, Dr. Carolina Martins Avila, Dr. Karin Juliane Pelizzaro-Rocha, Dr. Débora Barbosa Vendramini-Costa, Marina Pereira Dias, Dr. Daniela Barreto Barbosa Trivella, Prof. Dr. João Ernesto de Carvalho, Prof. Dr. Carmen Veríssima Ferreira-Halder and Prof. Dr. Ronaldo Aloise Pilli

    Article first published online: 25 AUG 2015 | DOI: 10.1002/cmdc.201500246

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    Fighting the big C: We describe the synthesis of a new family of analogues based on the scaffold of the natural product (−)-tarchonanthuslactone; these compounds were evaluated in vitro against tumor cell lines. We further conducted an initial investigation into the mechanism of action, including the inhibition of phosphatases and glutathione-S-transferase and the production of reactive oxygen species.

  4. Phage Selection of Bicyclic Peptide Ligands of the Notch1 Receptor

    Dr. Charlotte Urech-Varenne, Prof. Dr. Freddy Radtke and Prof. Dr. Christian Heinis

    Article first published online: 25 AUG 2015 | DOI: 10.1002/cmdc.201500261

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    Stabilizers on display: Bicyclic peptides that bind with high affinity to the negative regulatory region (NRR) of the Notch1 receptor were developed by phage display. The ligands were found to increase the melting temperature of the NRR, demonstrating that in-vitro-evolved bicyclic peptides can stabilize proteins.

  5. LASSBio-1829 Hydrochloride: Development of a New Orally Active N-Acylhydrazone IKK2 Inhibitor with Anti-inflammatory Properties

    Isabella A. Guedes, Rosana H. C. N. Freitas, Natália M. Cordeiro, Thaís S. do Nascimento, Tayna S. Valerio, Prof. Patrícia D. Fernandes, Prof. Laurent E. Dardenne and Prof. Carlos A. M. Fraga

    Article first published online: 25 AUG 2015 | DOI: 10.1002/cmdc.201500266

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    Quelling the kinase: IKK2 has been considered a good target for the design of novel drug prototypes to treat chronic inflammatory diseases. Herein we report the successful use of a structure-based drug design strategy for the development of LASSBio-1829 hydrochloride (10), an IKK2 inhibitor (IC50=3.8 μM) and a promising anti-inflammatory prototype.