puromycin and Leukemia-P388

puromycin has been researched along with Leukemia-P388* in 3 studies

Other Studies

3 other study(ies) available for puromycin and Leukemia-P388

ArticleYear
Synthesis and biological evaluation of 5'-sulfamoylated purinyl carbocyclic nucleosides.
    Journal of medicinal chemistry, 1992, Oct-30, Volume: 35, Issue:22

    The first series of 5'-sulfamoylated carbocyclic purinyl nucleosides was synthesized and tested for antitumor and antibacterial activities. The target compounds were formed by reacting the 2',3'-acetonide-protected carbocyclic nucleosides with sulfamoyl chloride, followed by deprotection. The agents were tested for cytotoxic activity against P388 mouse leukemia cells. Two compounds, 5'-sulfamoyl carbocyclic adenosine (2) and 5-sulfamoyl-8-aza carbocyclic adenosine (6) exhibited IC50 values as low as 62 and 15 nM, respectively. These analogs inhibited protein biosynthesis and slowed down DNA and RNA biosyntheses in the P388 cells. None of the target molecules were as potent against Escherichia coli as they were against the tumor cells. Also, in cell-free systems, agents 2 and 6 were more effective inhibitors of protein synthesis in rabbit reticulocyte lysate than in E. coli. These new carbocyclic derivatives appear to be somewhat selective for eukaryotic over prokaryotic cells in affecting translation.

    Topics: Adenosine; Adenosine Deaminase; AMP Deaminase; Animals; Anti-Bacterial Agents; Antimetabolites, Antineoplastic; Drug Screening Assays, Antitumor; Escherichia coli; In Vitro Techniques; Leukemia P388; Mice; Microbial Sensitivity Tests; Protein Synthesis Inhibitors; Rabbits; Tumor Cells, Cultured

1992
Carbocyclic puromycin: synthesis and inhibition of protein biosynthesis.
    Journal of medicinal chemistry, 1986, Volume: 29, Issue:11

    The carbocyclic analogue of puromycin was prepared by the coupling of N-(benzyloxycarbonyl)-p-methoxy-L-phenylalanine to the racemic aminonucleoside (+/-)-9-[3 beta-amino-2 beta-hydroxy-4 alpha-(hydroxymethyl)cyclopent-1 alpha-yl]-6-(dimethylamino)purine, followed by separation of the diastereomers and subsequent removal of the Cbz blocking group. Kinetic studies indicate that carbocyclic puromycin is an excellent substrate for the peptidyltransferase reaction with both prokaryotic and eukaryotic ribosomes. A comparison of carbocyclic puromycin with previously synthesized analogues indicate that the furanosyl ring oxygen and the hydroxymethyl group of puromycin do not contribute to ribosomal binding, but both moieties contribute to the rate of product formation from the enzyme-substrate complex. Carbocyclic puromycin was equal to puromycin when evaluated for cytotoxicity using P-388 mouse lymphoid leukemia cells in culture.

    Topics: Animals; Leukemia P388; Mice; Protein Biosynthesis; Puromycin; Ribosomes; Structure-Activity Relationship

1986
Synthesis and biological evaluation of sparsomycin analogues.
    Journal of medicinal chemistry, 1983, Volume: 26, Issue:11

    Three series of sparsomycin analogues were prepared and examined for their ability to inhibit DNA or protein synthesis in bone marrow, P388 lymphocytic leukemia, and P815 mastocytoma cells. The compounds of series I and II, distinguished by the inclusion or exclusion of a hydroxymethyl functional group, were designed to elucidate the effect on activity of replacing the oxodithioacetal side chain of sparsomycin with 4-substituted benzyl groups. The series III analogues, which excluded the hydroxymethyl group and replaced the oxodithioacetal moiety of sparsomycin with a benzyl amide group, were designed to investigate the potential interaction of an amide oxygen in contrast to the sulfoxide oxygen of sparsomycin. Overall, the bromobenzyl-substituted analogues imparted the greatest inhibitory activity in the protein synthesis assay, while the methoxybenzyl-substituted analogues displayed the least. The methylbenzyl and the unsubstituted benzyl compounds were intermediate in inhibitory potential. The activity in the protein synthesis assay may correspond to the lipophilic and electronic characteristics of the substituents on the benzyl moiety of the analogues. All of the compounds were inactive in the DNA synthesis assay.

    Topics: Animals; Antibiotics, Antineoplastic; Biological Assay; Bone Marrow; DNA Replication; Drug Evaluation, Preclinical; Indicators and Reagents; Leukemia P388; Male; Mast-Cell Sarcoma; Mice; Mice, Inbred DBA; Protein Biosynthesis; Sparsomycin; Structure-Activity Relationship

1983
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