Copyright © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
July 29, 2014
New Two-Year Impact Factor:
The Journal Citation Report numbers are out, and they reflect ChemMedChem's solid performance! With a new two-year impact factor of 3.046, the journal is showing its prominent position in the medicinal chemistry community. Thanks to our Editorial and International Advisory Board members, numerous peer reviewers, as well as authors for helping make this journal the success it is.
Recently Published Articles
- Dangling Ends Perturb the Stability of RNA Duplexes Responsive to Surrounding Conditions
Dr. Hisae Tateishi-Karimata, Dr. Smritimoy Pramanik, Prof. Shu-ichi Nakano, Prof. Daisuke Miyoshi and Prof. Naoki Sugimoto
Article first published online: 28 JUL 2014 | DOI: 10.1002/cmdc.201402167
Let′s talk about stability: In the presence of various cosolutes, RNA duplexes with dangling ends are significantly destabilized depending on the hydration type of the dangling ends, although the RNA duplexes are stabilized in the absence of cosolutes. It has been postulated that dangling ends stabilize helices; however, our results suggest that the stabilization is responsive to the surrounding conditions.
- Singly Modified Amikacin and Tobramycin Derivatives Show Increased rRNA A-Site Binding and Higher Potency against Resistant Bacteria
Dr. Richard J. Fair, Dr. Lisa S. McCoy, Dr. Mary E. Hensler, Bernice Aguilar, Prof. Dr. Victor Nizet and Prof. Dr. Yitzhak Tor
Article first published online: 23 JUL 2014 | DOI: 10.1002/cmdc.201402175
Irresistible! Amikacin and tobramycin are two clinically useful RNA-targeting aminoglycosides. Modified versions of these compounds showed equal to or better potency against certain resistant bacterial strains, while their eukaryotic cytotoxicity remained identical to that of the parent antibiotics.
- Conjugation to Albumin-Binding Molecule Tags as a Strategy to Improve Both Efficacy and Pharmacokinetic Properties of the Complement Inhibitor Compstatin
Dr. Yijun Huang, Dr. Edimara S. Reis, Dr. Patrick J. Knerr, Prof. Wilfred A. van der Donk, Dr. Daniel Ricklin and Prof. John D. Lambris
Article first published online: 23 JUL 2014 | DOI: 10.1002/cmdc.201402212
Two birds with one stone: Conjugates of the complement inhibitor compstatin and albumin-binding molecules were designed to improve the drug’s pharmacokinetic properties. The resulting chimera ABM2-Cp20 indeed showed improved plasma protein binding, yet also largely enhanced target affinity, producing the most potent compstatin analogue so far.
- Diaryl-Substituted Azolylthioacetamides: Inhibitor Discovery of New Delhi Metallo-β-Lactamase-1 (NDM-1)
Yi-Lin Zhang, Prof. Ke-Wu Yang, Ya-Jun Zhou, Alecander E. LaCuran, Prof. Peter Oelschlaeger and Prof. Michael W. Crowder
Article first published online: 22 JUL 2014 | DOI: 10.1002/cmdc.201402249
New inhibitors for NDM-1: Azolylthioacetamides 1–18 were obtained and all of them were found to be inhibitors of metallo-β-lactamases (MβLs) L1 (Ki<2 μM). Compounds 1–7, 9–13, and 16 are mixed inhibitors of NDM-1 (Ki<7 μM), and 2, 4, 5, and 7 are broad-spectrum inhibitors of all four tested MβLs: CcrA, NDM-1, ImiS, and L1 (Ki<52 μM). Docking studies revealed that 4 and 10 coordinate to the ZnII ion(s) via the triazole moiety, while other moieties interact with the conserved active site residues Lys224 or Ser221.
- Structural and Biochemical Studies of Actin in Complex with Synthetic Macrolide Tail Analogues
Dr. Jose H. Pereira, Dr. Chutima Petchprayoon, Dr. Alexander C. Hoepker, Dr. Nigel Moriarty, Dr. Sarah J. Fink, Dr. Giuseppe Cecere, Prof. Ian Paterson, Prof. Paul D. Adams and Prof. Gerard Marriott
Article first published online: 22 JUL 2014 | DOI: 10.1002/cmdc.201402150
Actin’ tough: The actin filament binding and severing activities of marine macrolides are located within the hydrophobic tail region of the molecule. The synthetic tail analogue GC-04 is shown to bind to G-actin with a dissociation constant of (132±13) nM. The structure of the actin–GC-04 complex reveals the mode of tail binding within the cleft between subdomains 1 and 3.