62029-79-2Relevant academic research and scientific papers
C-4 " substituted Macrolides compd.
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Paragraph 0028; 0029, (2016/10/08)
A useful novel compound that shows superior antibacterial activity also against erythromycin resistant bacteria, for example, resistant pneumococci, streptococci, mycoplasmas, and the like, against which sufficient antibacterial activity cannot be obtaine
2-Alkynyl-8-aryladenines possessing an amide moiety: Their synthesis and structure-activity relationships of effects on hepatic glucose production induced via agonism of the A2B adenosine receptor
Harada,Asano,Kawata,Inoue,Horizoe,Yasuda,Nagata,Murakami,Nagaoka,Kobayashi,Tanaka,Abe
, p. 2709 - 2726 (2007/10/03)
A series of 2-alkynyl-8-aryladenine derivatives bearing an amide moiety at the 9-position of adenine was synthesized. These analogues were evaluated for inhibitory activity on N-ethylcarboxamidoadenosine (NECA)-induced glucose production in primary cultured rat hepatocytes. The m-primary benzamide derivative 15f was the most potent compound (IC50 = 0.017 μM), being 15-fold more active than the corresponding 9-methyl derivative (1). Compound 15f showed 72- and 5.2-fold selectivity for human A2B receptor versus human A1 and A2A receptors, respectively. Structure-activity relationship (SAR) studies of the synthesized compounds indicated that a three-carbon linker, fixed in the form of a benzene ring, between the adenine core and the amide moiety is important for both A2B antagonistic activity and selectivity. The IC50 values in rat hepatocyte glucose assay correlated well with the IC50 values in cAMP assay using Chinese hamster ovary cells stably transfected with human A2B receptors (r2 = 0.94). The A1 and A2A affinities showed no correlation with the potency to inhibit NECA-induced glucose production. These results strongly support our previous conclusion that adenosine agonist-induced hepatic glucose production in rat hepatocytes is mediated through the A2B receptor.
Photo-induced electron transfer in small peptides: glycylalanine
Hill, Roger R.,Jeffs, Graham E.,Banaghan, Frank,McNally, Tony,Werninck, Alan R.
, p. 1595 - 1600 (2007/10/03)
Participation of the peptide bond in photoinduced electron transfer accounts for product distributions in the photolysis of XG dipeptides and predicts the possibility that the side-chain will be involved in similar reactions of GX dipeptides.Product analysis following exposure of aqueous glycyl-DL-alanine to UV radiation shows this prediction is fulfilled.Thus, unlike XG peptides, glycylalanine degrades to acetamide substantially without co-production of CO2 and to products where bonding in the side-chain is involved in relaxation of the intermediate diradical.At a lower pH, decarboxylation radicals from glycylalanine have the opportunity to disproportionate as well as dimerize, and this accounts satisfactorily for the difference in product distribution when compared with that from XG photolysis under the same conditions.
