m-Iodosylbenzoic acid – a convenient recyclable reagent for highly efficient aromatic iodinations

• Andreas Kirschning,
• Mekhman S. Yusubov,
• Roza Y. Yusubova,
• Ki-Whan Chi and
• Joo Y. Park

Beilstein J. Org. Chem. 2007, 3, No. 19, doi:10.1186/1860-5397-3-19

• Andreas Kirschning Mekhman S. Yusubov Roza Y. Yusubova Ki-Whan Chi Joo Y. Park Institut für Organische Chemie and Zentrum für Biomolekulare Wirkstoffchemie (BMWZ), Leibniz Universität Hannover, Schneiderberg 1B, D-30167 Hannover, Germany The Siberian State Medical University, 2 Moskovsky trakt

• ). Additionally, the work was funded by the Fonds der Chemischen Industrie. Ki-Whan Chi thanks the University of Ulsan Research Fund 2006. We are grateful to Prof. Viktor Filimonov from Tomsk Polytechnic University for helpful discussions.

8-epi-Salvinorin B: crystal structure and affinity at the κ opioid receptor

• Thomas A. Munro,
• Katharine K. Duncan,
• Richard J. Staples,
• Wei Xu,
• Lee-Yuan Liu-Chen,
• Cécile Béguin,
• William A. Carlezon Jr. and
• Bruce M. Cohen

Beilstein J. Org. Chem. 2007, 3, No. 1, doi:10.1186/1860-5397-3-1

• ) itself, whose binding affinity (Ki = 43 nM) was reportedly greater than that of the natural epimer 2a (111 nM).[8] To explore this anomaly, we submitted a new sample of 2b for in vitro testing at the KOR. Binding affinity, potency and efficacy were determined as previously described (Table 1).[26] The

• binding affinity of 2b (Ki = 304 nM) was lower than those previously reported for salvinorin B (2a) under the same conditions (66, 111 or 155 nM).[7][8][27] An early report that 2a was inactive employed a different radiolabeled ligand, [3H]bremazocine.[28] Subsequent testing with [3H]diprenorphine by the

• same group gave concordant values for the relative affinity of 2a.[17] Thus, our data suggest that 2b in fact has a lower affinity than 2a, consistent with the general trend mentioned above. We also reexamined the epimeric acids 4.[16] In a previous report, 4a was found to be inactive (Ki > 1,000 nM

Synthesis and glycosidase inhibitory activity of new hexa- substituted C8-glycomimetics

• Olivia Andriuzzi,
• Christine Gravier-Pelletier,
• Gildas Bertho,
• Thierry Prangé and
• Yves Le Merrer

Beilstein J. Org. Chem. 2005, 1, No. 12, doi:10.1186/1860-5397-1-12

• towards glycosidases, while the core structure and essential network of hydroxyl functionalities for enzyme recognition are retained. An important example is the 1-deoxynojirimycin (DNJ) family, for which DNJ itself is a competitive inhibitor of α-D-glucosidase (Ki = 8–25 μM),[10] while its derivatives