160880-37-5Relevant academic research and scientific papers
Inhibitors for human glutaminyl cyclase by structure based design and bioisosteric replacement
Buchholz, Mirko,Hamann, Antje,Aust, Susanne,Brandt, Wolfgang,B?hme, Livia,Hoffmann, Torsten,Schilling, Stephan,Demuth, Hans-Ulrich,Heiser, Ulrich
experimental part, p. 7069 - 7080 (2010/05/02)
The inhibition of human glutaminyl cyclase (hQC) has come into focus as a new potential approach for the treatment of Alzheimer's disease. The hallmark of this principle is the prevention of the formation of Aβ 3,11(pE)-40,42, as these Aβ-speci
α1-Adrenoceptor blocking activity of some ring-open analogues of prazosin
Boschi,Di Stilo,Fruttero,Medana,Sorba,Gasco
, p. 661 - 667 (2007/10/02)
Synthesis and structural characterization of some ring-open analogues of Prazosin containing either the guanidine substructure or urea-equivalent groups are described. The opening of the pyrimidine ring in Prazosin is very important as far as the affinity for α1-adrenoceptor is concerned. The pA2 values of the ring-open derivatives are 104-105 fold lower than that of the parent. It is probable that the affinity decrease principally reflects a negative influence of the conformational factors in the interaction with the α1-receptor. The derivative 5 containing the guanidine moiety, charged at physiological pH, is as active as the other derivatives containing the uncharged urea-equivalent groups. This behaviour indicates, in this class of compounds, the importance of H-bonding interactions with the receptor. When in the ring-open models the ethanediamino substructure is substituted for the piperazine ring additional decrease in activity occurs.
