© WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
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
June 26, 2015
Editor's Picks: Issue 07/2015
Editor's picks for issue 07: In this issue, a Minireview by Matteo Masetti et al. and a Full Paper by Stefan Günther, Irmgard Merfort, and colleagues illustrate how the latest advances in computational chemistry are solving problems in drug design and discovery. Read more...
Recently Published Articles
- Influence of the Multivalency of Ultrashort Arg-Trp-Based Antimicrobial Peptides (AMP) on Their Antibacterial Activity
Barbara C. Hoffknecht, Dennis J. Worm, Sandra Bobersky, Pascal Prochnow, Prof. Dr. Julia E. Bandow and Prof. Dr. Nils Metzler-Nolte
Article first published online: 6 JUL 2015 | DOI: 10.1002/cmdc.201500220
More than the sum of its parts: The antibacterial activities of 15 new antimicrobial peptides on five different bacterial strains were tested, including an MRSA strain. With ultrashort peptides a clear synergistic effect of the trivalent display was observed. The best candidates showed activities in the low-micromolar range against Gram-positive MRSA and Gram-negative A. baumannii, with only minimal hemolytic activity against red blood cells.
- Therapeutic Developments Targeting Toll-like Receptor-4-Mediated Neuroinflammation
Dr. Jing Li, Adam Csakai, Jialin Jin, Prof. Fengchun Zhang and Prof. Hang Yin
Article first published online: 1 JUL 2015 | DOI: 10.1002/cmdc.201500188
Pain management: Toll-like receptors (TLRs) are a family of membrane proteins crucial to the cellular innate immune response. Pain is one of the most intractable and widespread conditions that people face today. At the crossroads of the immune system and pain is TLR4. This review provides a brief summary of TLRs and how their signaling affects pain. Moreover, this review takes a look at the molecules that are able to modulate TLR4 signaling as potential drug candidates.
- Bisamidate Prodrugs of 2-Substituted 9-[2-(Phosphonomethoxy)ethyl]adenine (PMEA, adefovir) as Selective Inhibitors of Adenylate Cyclase Toxin from Bordetella pertussis
Dr. Michal Česnek, Dr. Petr Jansa, Dr. Markéta Šmídková, Dr. Helena Mertlíková-Kaiserová, Dr. Martin Dračínský, Tarsis F. Brust, Prof. Petr Pávek, Dr. František Trejtnar, Prof. Val J. Watts and Dr. Zlatko Janeba
Article first published online: 1 JUL 2015 | DOI: 10.1002/cmdc.201500183
Whooping cough combatted: With the aim to establish a new strategy against pertussis, C2-modified adefovir analogues in their bisamidate prodrug form were found to efficiently inhibit adenylate cyclase toxin (ACT) from Bordetella pertussis. The compounds show favorable plasma stability, effective distribution to target tissues, and good selectivity for ACT over human adenylate cyclase isoforms.
- Active Site Mapping of Human Cathepsin F with Dipeptide Nitrile Inhibitors
Janina Schmitz, Norbert Furtmann, Moritz Ponert, Dr. Maxim Frizler, Dr. Reik Löser, Prof. Dr. Ulrike Bartz, Prof. Dr. Jürgen Bajorath and Prof. Dr. Michael Gütschow
Article first published online: 26 JUN 2015 | DOI: 10.1002/cmdc.201500151
Mapping with nitriles: For human cathepsin F, low-molecular-weight inhibitors have not been developed so far. Therefore, a library of 52 dipeptide nitriles, known to interact in a covalent but reversible manner with the active site cysteine, was evaluated for cathepsin F inhibition. With the kinetic data in hand, optimized candidates were designed, synthesized, and tested to improve the activity profile as cathepsin F inhibitors.
- nido-Dicarbaborate Induces Potent and Selective Inhibition of Cyclooxygenase-2
Dr. Wilma Neumann, Dr. Shu Xu, Dr. Menyhárt B. Sárosi, Dr. Matthias S. Scholz, Brenda C. Crews, Kebreab Ghebreselasie, Dr. Surajit Banerjee, Prof. Dr. Lawrence J. Marnett and Prof. Dr. Dr. h.c. Evamarie Hey-Hawkins
Article first published online: 18 JUN 2015 | DOI: 10.1002/cmdc.201500199
Potency boost: Replacement of a phenyl moiety in indomethacin with a nido-dicarbaborate group results in a compound with a novel binding mode and markedly increased inhibitory activity and selectivity for COX-2, with a concomitant increase in stability and water solubility, while maintaining strong hydrophobic interactions in the binding site of the enzyme. This shows nido-dicarbaborate to be a promising pharmacophore for a variety of inhibitors.