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• 54653-62-2 N-β-alanyldopamine 

Relevant academic research and scientific papers

Selective inhibition of Src protein tyrosine kinase by analogues of 5- S-glutathionyl-β-alanyl-L-dopa

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).

Model insect cuticle sclerotization: Reactions of catecholamine quinones with the nitrogen-centered nucleophiles imidazole and N-acetylhistidine

The catecholamines N-acetyldopamine (NADA) and N-β-alanyldopamine (NBAD) are two precursors for quinonoios used as sclerotizing agents in insect cuticle. This study focused on the reaction pathways of the quinones of NADA and NBAD by using two nitrogencen

Screening test for insecticides interfering with cuticular sclerotization

The potential of known and new insecticides to interfere with cuticle sclerotization was investigated using assays for key enzymes such as phenoloxidase, quinone methide isomerase and DOPA decarboxylase. Homogenates from the blowfly Lucilia cuprina and from the epithelial cell line from Chironomus tentans were used to examine the compounds under investigation. Phenoloxidases are known to oxidize DOPA, the substrate for DOPA decarboxylase. Since phenoloxidases were not detectable in C. tentans cell homogenates, inhibitor and kinetic studies were done for comparison with DOPA decarboxylase of this insect cell line. DOPA decarboxylase and phenoloxidase of L. cuprina exerted highest specific activities at early pupal stages (day 7). The apparent K(m) values for the two enzymes were 0.47(±0-21) mM and 0.71(±0.16) mM, respectively, using L-DOPA as substrate. DOPA decarboxylase from C. tentans had a K(m) value of 0.42(±0.18) mM. Quinone methide isomerase was most active in young pupae. In terms of substrate specificity for enzymic (mushroom-tyrosinase) production of different quinones from their corresponding catechols, that with dopamine quinone proved to be the most efficient. Synthesis of derivatives of L-DOPA and L-tyrosine led to a compound which inhibited both phenoloxidase and quinone methide isomerase. DOPA decarboxylase from L. cuprina and from cells of C. tentans was inhibited by carbidopa (IC50 values of 0.021(±0.011) μM and 0.031(±0.019) μM, respectively) and indomethacine (IC50 values of 22.6(±7.1) μM and 18.8(±9.7) μM). Both compounds exerted a competitive type of inhibition and were able to interfere with development of L. cuprina.