313045-70-4Relevant academic research and scientific papers
Structure-based design and synthesis of phosphinate isosteres of phosphotyrosine for incorporation in Grb2-SH2 domain inhibitors. Part 1
Furet, Pascal,Caravatti, Giorgio,Denholm, Alastair A.,Faessler, Alex,Fretz, Heinz,Garcia-Echeverria, Carlos,Gay, Brigitte,Irving, Ed,Press, Neil J.,Rahuel, Joseph,Schoepfer, Joseph,Walker, Clive V.
, p. 2337 - 2341 (2007/10/03)
Based on X-ray crystal structure information, mono charged phosphinate isosteres of phosphotyrosine have been designed and incorporated in a short inhibitory peptide sequence of the Grb2-SH2 domain. The resulting compounds, by exploiting additional interactions, inhibit binding to the Grb2-SH2 domain as potently as the corresponding doubly charged (phosphonomethyl)phenylalanine analogue. (C) 2000 Elsevier Science Ltd.
1, 2-Disubstituted cyclohexane derived tripeptide aldehydes as novel selective thrombin inhibitors
Harmat, Nicholas J.S.,Di Bugno, Cristina,Criscuoli,Giorgi, Raffaello,Lippi, Annalisa,Martinelli, Adriano,Monti, Susanna,Subissi
, p. 1249 - 1254 (2007/10/03)
A series of tripeptide arginine aldehydes was synthesized by replacement of proline with 1,2-disubstituted cyclohexane derivatives in the sequence of D-MePhe-Pro-Arg-H. Based on molecular modeling, further modification of the D-MePhe residue resulted in a potent and selective thrombin inhibitor.
