853934-74-4Relevant academic research and scientific papers
Discovery of β-homophenylalanine based pyrrolidin-2-ylmethyl amides and sulfonamides as highly potent and selective inhibitors of dipeptidyl peptidase IV
Nordhoff, Sonja,Cerezo-Galvez, Silvia,Deppe, Holger,Hill, Oliver,Lopez-Canet, Meritxell,Rummey, Christian,Thiemann, Meinolf,Matassa, Victor G.,Edwards, Paul J.,Feurer, Achim
scheme or table, p. 4201 - 4203 (2010/04/02)
Modifications of DPP-4 inhibitor 5, that was discovered by structure based design, are described and structure-activity relationships discussed. With analogue 7k one of the most potent non-covalent inhibitors of DPP-4 reported to date (IC50 = 0.38 nM) was discovered. X-ray structure of inhibitor 7k bound to DPP-4 revealed a hydrogen bonding interaction with Q553. First successful efforts in balancing overall properties, as demonstrated by improved metabolic stability, highlight the potential of this series.
The reversed binding of β-phenethylamine inhibitors of DPP-IV: X-ray structures and properties of novel fragment and elaborated inhibitors
Nordhoff, Sonja,Cerezo-Galvez, Silvia,Feurer, Achim,Hill, Oliver,Matassa, Victor G.,Metz, Guenther,Rummey, Christian,Thiemann, Meinolf,Edwards, Paul J.
, p. 1744 - 1748 (2007/10/03)
The co-crystal structure of β-phenethylamine fragment inhibitor 5 bound to DPP-IV revealed that the phenyl ring occupied the proline pocket of the enzyme. This finding provided the basis for a general hypothesis of a reverse binding mode for β-phenethylam
DPP-IV INHIBITORS
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Page/Page column 22-23, (2010/02/11)
The invention relates to compounds of formula (I) wherein Z, R1-5, X, n, A1 and A2 have the meaning as cited in the description and the claims. Said compounds are useful as DPP-IV inhibitors. The invention also relates to
