357649-93-5

Usage

Uses

Used in Pharmaceutical Industry:
Histone Acetyltransferase Inhibitor IV, CPTH2 is used as an anticancer agent for its potential role in modulating Gcn5p dependent functional networks in vitro and in vivo. It targets the deregulated histone acetyltransferases (HAT) and histone deacetylases (HDAC) activity, which plays a role in the development of various cancers.
Used in Research Applications:
Histone Acetyltransferase Inhibitor IV, CPTH2 is used as a research tool for the inhibition of histone acetyltransferase in cortical cultures, bud cells, and natural killer T cells (iNKT) to study the effects of histone acetylation on chromatin structure and gene expression.

Biochem/physiol Actions

CPTH2 is a histone acetyltransferase (HAT) inhibitor modulating the Gcn5 network. Histone Acetyltransferase (HAT) inhibitor modulating Gcn5 network. Histone acetyltransferases (HATs) act as transcriptional coactivators. Histone acetylation plays an important role in regulating the chromatin structure and is tightly regulated by two classes of enzyme, histone acetyltransferases (HAT) and histone deacetylases (HDAC). Deregulated HAT and HDAC activity plays a role in the development of a range of cancers. Consequently, inhibitors of these enzymes have potential as anticancer agents.

References

1) Chimenti?et al. (2009),?A novel histone acetyltransferase inhibitor modulating Gcn5 network: cyclopentylidene-[4-(4′-chlorophenyl)thiazol-2-yl]hydrazone); J. Med .Chem.,?52?530

Upstream product

• 7283-39-8 cyclopentanone thiosemicarbazone 
• 536-38-9 4-chlorobenzoylmethyl bromide 

Relevant academic research and scientific papers

Application of alicyclic ketone hydrazone thiazole derivative serving as tyrosinase inhibitor

The invention discloses an alicyclic ketone hydrazone thiazole derivative having tyrosinase inhibiting activity. Screening results of in-vitro inhibition tyrosinase show that the synthesized derivative has the tyrosinase inhibiting activity. The compound

Synthesis, semipreparative HPLC separation, biological evaluation, and 3D-QSAR of hydrazothiazole derivatives as human monoamine oxidase B inhibitors

The present study reports on synthesis in high yields (70-99%), HPLC enantioseparation, inhibitory activity against human monoamino oxidases, and molecular modeling including 3D-QSAR studies, of a large series of (4-aryl-thiazol-2-yl)hydrazones (1-45). Most of the synthesized compounds proved to be potent and selective inhibitors of hMAO-B isoform in the micromolar or nanomolar range, thus demonstrating that hydrazothiazole could be considered a good pharmacophore to design new hMAO-B inhibitors. Due to the presence in some derivatives of a chiral center, we also performed a semipreparative chromatographic enantioseparation of these compounds obtained by a stereoconservative pattern. The separated enantiomers were submitted to in vitro biological evaluation to point out the stereorecognition of the active site of the enzyme towards these structures. Finally, a 3D-QSAR study was carried out using Comparative Molecular Field Analysis (CoMFA), aiming to deduce rational guidelines for the further structural modification of these lead compounds.

Synthesis and in vitro activity of 2-thiazolylhydrazone derivatives compared with the activity of clotrimazole against clinical isolates of Candida spp.

In this paper, we report on the synthesis of a novel series of 2-thiazolylhydrazone derivatives and the influence of the substituents on the thiazole ring on antifungal activity. All synthesized compounds were screened for their in vitro activities agains