142995-32-2Relevant academic research and scientific papers
Design and Combinatorial Development of Shield-1 Peptide Mimetics Binding to Destabilized FKBP12
Bols, Mikael,Diness, Frederik,J?rgensen, Frederik P.,Madsen, Daniel,Meldal, Morten,Olsen, Jakob V.,Palmer, Daniel,Roux, Milena E.,Schoffelen, Sanne
supporting information, (2020/03/10)
On the basis of computational design, a focused one-bead one-compound library has been prepared on microparticle-encoded PEGA1900 beads consisting of small tripeptides with a triazole-capped N-terminal. The library was screened towards a double
Studies of Neurokinin Antagonists. 4. Synthesis and Structure-Activity Relationships of Novel Dipeptide Substance P Antagonists: N2--L-prolyl>-N-methyl-N-(phenylmethyl)-3-(2-naphthyl)-L-alaninamide and Its Related Compounds
Hagiwara, Daijiro,Miyake, Hiroshi,Igari, Norihiro,Karino, Masako,Maeda, Yasue,et al.
, p. 2090 - 2099 (2007/10/02)
As an extension of our studies on discovering a novel substance P (SP) antagonist, we modified the previously reported dipeptide, N2-2-(1H-indol-3-ylcarbonyl)-L-lysyl>-N-methyl-N-(phenylmethyl)-L-phenylalaninamide (2b).The lysine part in 2b was first optimized to a (2S,4R)-hydroxyproline derivative (3h), which is 2-fold more potent than 2b in SP binding assay using guinea pig lung membranes.Next we modified the 1H-indol-3-ylcarbonyl part in 3h.Introduction of a methyl group at the indole nitrogen enhanced the oral activity, while retaining the binding activity.Finally, we modified the phenylalanine part to culminate in the most potent compound 7k (FK888), which is a potent SP antagonist with NK1 selectivity as well as oral activity.
