An absolute structure template for a unique voltage-gated sodium channel binding site
Palmer, Rex A., Potter, Brian S., Leach, Michael J., Jenkins, Terence C. and Chowdhry, Babur Z. (2010) An absolute structure template for a unique voltage-gated sodium channel binding site. MedChemComm, 1 (1). pp. 45-49. ISSN 2040-2503 (Print), 2040-2511 (Online) (doi:10.1039/C0MD00043D)Full text not available from this repository.
The X-ray crystallographic structures of the mesylate salts of a novel voltage-gated sodium channelbinding ligand R-(-)-BW202W92 and its much less active S-(+)-enantiomer (BW203W92) have beendetermined to establish their absolute configurations. Each enantiomer exists as two distinct atropisomeric forms in the solid state and the crystal structures for each enantiomer are stabilized by quite distinct patterns of intermolecular hydrogen bonding. Such structural differences will influence the pharmacological properties of the enantiomers and hence dictate their contrasting receptor binding properties.
|Additional Information:|| First published online: 9th June 2010.  First published in print: July 1 2010.  Published as: Med. Chem. Commun., 2010, 1, (1), 45-49.  Electronic supplementary information (ESI) available: Experimental details and Supplementary tables. CCDC reference numbers 299482, 299483. For ESI and crystallographic data in CIF or other electronic format see DOI: 10.1039/c0md00043d.  MedChemComm is the official journal of the European Federation for Medicinal Chemistry (EFMC).|
|Uncontrolled Keywords:||voltage-gated sodium channels, BW202W92, BW203W92, X-ray crystallographic structures|
|Subjects:||Q Science > QD Chemistry
T Technology > TP Chemical technology
|School / Department / Research Groups:||School of Science
Faculty of Engineering & Science > School of Science
School of Science > Department of Life & Sports Science
Faculty of Engineering & Science > School of Science > Department of Life & Sports Science
|Last Modified:||24 May 2013 11:05|
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