| Structural highlights
Publication Abstract from PubMed
A new class of p38alpha inhibitors based on a biaryl-triazolopyridine scaffold was investigated. X-ray crystallographic data of the initial lead compound cocrystallised with p38alpha was crucial in order to uncover a unique binding mode of the inhibitor to the hinge region via a pair of water molecules. Synthesis and SAR was directed towards the improvement of binding affinity, as well as ADME properties for this new class of p38alpha inhibitors and ultimately afforded compounds showing good in vivo efficacy.
Novel triazolopyridylbenzamides as potent and selective p38alpha inhibitors.,Aiguade J, Balague C, Carranco I, Caturla F, Dominguez M, Eastwood P, Esteve C, Gonzalez J, Lumeras W, Orellana A, Preciado S, Roca R, Vidal L, Vidal B Bioorg Med Chem Lett. 2012 May 15;22(10):3431-6. doi: 10.1016/j.bmcl.2012.03.099., Epub 2012 Apr 4. PMID:22521646[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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References
- ↑ Aiguade J, Balague C, Carranco I, Caturla F, Dominguez M, Eastwood P, Esteve C, Gonzalez J, Lumeras W, Orellana A, Preciado S, Roca R, Vidal L, Vidal B. Novel triazolopyridylbenzamides as potent and selective p38alpha inhibitors. Bioorg Med Chem Lett. 2012 May 15;22(10):3431-6. doi: 10.1016/j.bmcl.2012.03.099., Epub 2012 Apr 4. PMID:22521646 doi:10.1016/j.bmcl.2012.03.099
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