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.
Peptidyl epoxides extended in the P′ direction as cysteine protease inhibitors: Effect on affinity and mechanism of inhibition
Perlman, Nurit,Hazan, Maya,Shokhen, Michael,Albeck, Amnon
experimental part, p. 9032 - 9039 (2009/04/04)
Endo peptidyl epoxides, in which the central epoxidic moiety replaces the scissile amide bond of a P3-P3′ peptide, were designed as cysteine proteases inhibitors. The additional P′-S′ interactions, relative to those of an exo peptidyl epoxide of the same P3-P1 sequence, significantly improved affinity to the enzymes papain and cathepsin B, but also changed the mode of inhibition from active-site directed inactivation to reversible competitive inhibition. Computational models rationalize the binding affinity and the inhibition mechanism.