1228019-38-2Relevant academic research and scientific papers
Development and evaluation of novel phosphotyrosine mimetic inhibitors targeting the Src homology 2 domain of signaling lymphocytic activation molecule (SLAM) associated protein
Chu, Chi-Yuan,Chang, Chun-Ping,Chou, Yun-Ting,Handoko,Hu, Yi-Ling,Lo, Lee-Chiang,Lin, Jing-Jer
, p. 2841 - 2849 (2013)
Specific interactions between Src homology 2 (SH2) domain-containing proteins and the phosphotyrosine-containing counterparts play significant role in cellular protein tyrosine kinase (PTK) signaling pathways. The SH2 domain inhibitors could potentially serve as drug candidates in treating human diseases. Here we have incorporated a novel phosphotyrosine mimetic, which is an unusual amino acid carrying a cyclosaligenyl (cycloSal) phosphodiester moiety, into dipeptides to investigate the inhibitory effect on SH2 domain-containing proteins. A plate-based assay was also established to screen for inhibitors that disrupt the interaction between a phosphopeptide of SLAM (signaling lymphocytic activation molecule) and its interacting protein SAP (SLAM-associated protein). We identified a number of inhibitors with IC50 values in the range of 17-35 μM, implying that the cycloSal phosphodiester-carrying amino acid could mimic the phosphotyrosyl residue. Our results also raise the possibility of integrating the newly developed phosphotyrosine mimetic moiety into inhibitors designed for other SH2 domain-containing proteins.
Construction of the cyclophane core of the hirsutellones via a RCM strategy
Huang, Mingzheng,Song, Liqiang,Liu, Bo
supporting information; experimental part, p. 2504 - 2507 (2010/07/05)
Construction of the highly strained [10]-paracyclophane core of the hirsutellones has been completed via an effective RCM strategy.
