853934-65-3Relevant academic research and scientific papers
Systematic evaluation of a few proline derivatives as catalysts for a direct aldol reaction
Sutar, Revannath L.,Joshi, Navalkishore N.
, p. 43 - 49 (2013/02/23)
A series of pyrrolidine derivatives were prepared and examined as catalysts for an aldol reaction. Structural variations in these molecules involved altering the sterics at the α-position, the position of the carbonyl group, and the acidities of the hydrogen bonding sites. The effect of these factors on catalytic activity and enantioselectivity was studied. The experimental results revealed that additional sterics at the α-position were detrimental. However, no correlation was found between the catalytic activity and N-H acidity.
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
