41036-19-5Relevant articles and documents
Synthesis and cellular effects of novel 1,3,5-triazine derivatives in DLD and Ht-29 human colon cancer cell lines
Wróbel, Agnieszka,Kolesińska, Beata,Fr?czyk, Justyna,Kamiński, Zbigniew J.,Tankiewicz-Kwedlo, Anna,Hermanowicz, Justyna,Czarnomysy, Robert,Maliszewski, Dawid,Drozdowska, Danuta
, p. 990 - 1002 (2019/11/03)
This study provides new information on the cellular effects of 1,3,5-triazine nitrogen mustards with different peptide groups in DLD and Ht-29 human colon cancer cell lines. A novel series of 2,4,6-trisubstituted 1,3,5-triazine derivatives bearing 2-chloroethyl and oligopeptide moieties was designed and synthesized. The most cytotoxic derivative was triazine with an Ala-Ala-OMe substituent on the ring (compound 7b). This compound induced time- and dose-dependent cytotoxicity in the DLD-1 and HT-29 colon cancer cell lines. The triazine derivative furthermore induced apoptosis through intracellular signaling pathway attenuation. Compound 7b may be a candidate for further evaluation as a chemotherapeutic agent against colorectal cancer.
Substrate derived peptidic α-ketoamides as inhibitors of the malarial protease PfSUB1
Kher, Samir S.,Penzo, Maria,Fulle, Simone,Finn, Paul W.,Blackman, Michael J.,Jirgensons, Aigars
supporting information, p. 4486 - 4489 (2015/02/19)
Peptidic α-ketoamides have been developed as inhibitors of the malarial protease PfSUB1. The design of inhibitors was based on the best known endogenous PfSUB1 substrate sequence, leading to compounds with low micromolar to submicromolar inhibitory activity. SAR studies were performed indicating the requirement of an aspartate mimicking the P1′ substituent and optimal P1-P4length of the non-prime part. The importance of each of the P1-P4amino acid side chains was investigated, revealing crucial interactions and size limitations.
Syntheses of the P-methylase substrates of the bialaphos biosynthetic pathway
Xiao, Youli,Lee, Kent,Liu, Pinghua
supporting information; experimental part, p. 5521 - 5524 (2009/06/28)
(Chemical Equation Presented) Genetic studies suggest that either N-acetyldemethyl phosphinothricin (1, N-AcDMPT) or N-acetyldemethyl phosphinothricin tripeptide (2, N-AcDMPTT) is the substrate for the P-methylation reaction in the biosynthesis of phosphinothricin tripeptide (PTT), which is widely used as an herbicide. To study the mechanism for this unique P-methylation reaction catalyzed by the BcpD protein and the functions of the unusual nonribosomal peptide synthetases involved in PTT biosynthesis, this work reports the chemical syntheses of 1 and 2.