177746-81-5Relevant articles and documents
Inhibition effects of 5-S-glutathionyl-N-β-alanyl-L-dopa analogues against Src protein tyrosine kinase
Zheng, Zhe-Bin,Nagai, Sachie,Iwanami, Naoko,Kobayashi, Ayako,Natori, Shunji,Sankawa, Ushio
, p. 777 - 782 (1999)
Twelve analogues of the antibacterial phenolic peptide 5-S- glutathionyl-N-β-alanyl-L-dopa (5-S-GA-L-D, 1) were synthesized via orthoquinone using tyrosinase. Several synthesized compounds inhibited the v- Src autophosphorylation tyrosine kinase reaction with an IC50 value comparable to that of herbimycin A. The inhibition of c-Src substrate phosphorylation was much less active than v-Src autophosphorylation inhibition. 5-S-GAL-D (1) and its analogous competed with peptide substrate and non-competed with ATP. The analogues showed no effects on substrate phosphorylation by epidermal growth factor receptor (EGFR), and this selectivity is the most characteristic feature of the 5-S-GA-L-D and its analogues (1 - 12).
Selective inhibition of Src protein tyrosine kinase by analogues of 5- S-glutathionyl-β-alanyl-L-dopa
Zheng, Zhe-Bin,Nagai, Sachie,Iwanami, Naoko,Kobayashi, Ayako,Hijikata, Mariko,Natori, Shunji,Sankawa, Ushio
, p. 1950 - 1951 (2007/10/03)
Twelve analogues of the antibacterial phenolic peptide 5-S- glutathionyl-β-alanyl-L-dopa (5-S-GA-L-D: 1) were synthesized via orthoquinones using tyrosinase. Several synthesized compounds inhibited the v-Src autophosphorylation tyrosine kinase reaction with an IC50 value comparable to that of herbimycin. The inhibition of c-Src substrate phosphorylation was much less active than v-Src autophosphorylation inhibition. The analogues showed no effects on substrate phosphorylation by epidermal growth factor receptor (EGFR), and this selectivity is the most characteristic feature of the analogues (1-12).