| Literature DB >> 23151054 |
Matthew C Lucas1, David M Goldstein, Johannes C Hermann, Andreas Kuglstatter, Wenjian Liu, Kin Chun Luk, Fernando Padilla, Michelle Slade, Armando G Villaseñor, Jutta Wanner, Wenwei Xie, Xiaohu Zhang, Cheng Liao.
Abstract
A novel approach to design selective spleen tyrosine kinase (Syk) inhibitors is described. Inhibition of spleen tyrosine kinase has attracted much attention as a mechanism for the treatment of autoimmune diseases such as asthma, rheumatoid arthritis, and SLE. Fostamatinib, a Syk inhibitor that successfully completed phase II clinical trials, also exhibits some undesirable side effects. More selective Syk inhibitors could offer safer, alternative treatments. Through a systematic evaluation of the kinome, we identified Pro455 and Asn457 in the Syk ATP binding site as a rare combination among sequence aligned kinases and hypothesized that optimizing the interaction between them and a Syk inhibitor molecule would impart high selectivity for Syk over other kinases. We report the structure-guided identification of three series of selective spleen tyrosine kinase inhibitors that support our hypothesis and offer useful guidance to other researchers in the field.Entities:
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Year: 2012 PMID: 23151054 DOI: 10.1021/jm301367c
Source DB: PubMed Journal: J Med Chem ISSN: 0022-2623 Impact factor: 7.446