551921-12-1

Basic information

• Product Name: 1-(4-PYRIDINYL)-1-ETHANONE N-[4-(4-CHLOROPHENYL)-1,3-THIAZOL-2-YL]HYDRAZONE
• Synonyms: 1-(4-PYRIDINYL)-1-ETHANONE N-[4-(4-CHLOROPHENYL)-1,3-THIAZOL-2-YL]HYDRAZONE
• CAS NO: 551921-12-1
• Molecular Formula: C₁₆H₁₃ClN₄S
• Molecular Weight: 328.82
• Mol File: 551921-12-1.mol

Chemical Properties

• Appearance: /
• CAS DataBase Reference: 1-(4-PYRIDINYL)-1-ETHANONE N-[4-(4-CHLOROPHENYL)-1,3-THIAZOL-2-YL]HYDRAZONE(CAS DataBase Reference)
• NIST Chemistry Reference: 1-(4-PYRIDINYL)-1-ETHANONE N-[4-(4-CHLOROPHENYL)-1,3-THIAZOL-2-YL]HYDRAZONE(551921-12-1)
• EPA Substance Registry System: 1-(4-PYRIDINYL)-1-ETHANONE N-[4-(4-CHLOROPHENYL)-1,3-THIAZOL-2-YL]HYDRAZONE(551921-12-1)

Safety Data

• Hazardous Substances Data: 551921-12-1(Hazardous Substances Data)

Usage

Type of compound

Hydrazone derivative

Potential properties

Anti-inflammatory and anti-cancer

Application

Treatment of various inflammatory diseases and cancer, including colorectal cancer

Mechanism of action

Inhibits the activity of certain enzymes and signaling pathways involved in inflammation and tumor progression

Current status

Ongoing research to explore full potential in the field of medicine

Upstream product

• 536-38-9 4-chlorobenzoylmethyl bromide 
• 3115-21-7 2-(1-(pyridin-4-yl)ethylidene)hydrazinecarbothioamide 
• 1122-54-9 methyl (4-pyridyl) ketone 
• 937-20-2 p-chlorophenacyl chloride 

Relevant articles and documents

(Thiazol-2-yl)hydrazone derivatives from acetylpyridines as dual inhibitors of MAO and AChE: Synthesis, biological evaluation and molecular modeling studies

Several (thiazol-2-yl)hydrazone derivatives from 2-, 3- and 4-acetylpyridine were synthesized and tested against human monoamine oxidase (hMAO) A and B enzymes. Most of them had an inhibitory effect in the low micromolar/high nanomolar range, being derivatives of 4-acetylpyridine selective hMAO-B inhibitors also at low nanomolar concentrations. The structure-activity relationship, as confirmed by molecular modeling studies, proved that the pyridine ring linked to the hydrazonic nitrogen and the substituted aryl moiety at C4 of the thiazole conferred the inhibitory effects on hMAO enzymes. Successively, the strongest hMAO-B inhibitors were tested toward acetylcholinesterase (AChE) and the most interesting compound showed activity in the low micromolar range. Our results suggest that this scaffold could be further investigated for its potential multi-targeted role in the discovery of new drugs against the neurodegenerative diseases.

Evaluation of a large library of (thiazol-2-yl)hydrazones and analogues as histone acetyltransferase inhibitors: Enzyme and cellular studies

Recently we described some (thiazol-2-yl)hydrazones as antiprotozoal, antifungal and anti-MAO agents as well as Gcn5 HAT inhibitors. Among these last compounds, CPTH2 and CPTH6 showed HAT inhibition in cells and broad anticancer properties. With the aim to identify HAT inhibitors more potent than the two prototypes, we synthesized several new (thiazol-2-yl)hydrazones including some related thiazolidines and pyrimidin-4(3H)-ones, and we tested the whole library existing in our lab against human p300 and PCAF HAT enzymes. Some compounds (1x, 1c', 1d', 1i' and 2m) were more efficient than CPTH2 and CPTH6 in inhibiting the p300 HAT enzyme. When tested in human leukemia U937 and colon carcinoma HCT116 cells (100 μM, 30 h), 1x, 1i' and 2m gave higher (U937 cells) or similar (HCT116 cells) apoptosis than CPTH6, and were more potent than CPTH6 in inducing cytodifferentiation (U937 cells).

Synthesis of a novel series of thiazole-based histone acetyltransferase inhibitors

Acetylation, which targets a broad range of histone and non-histone proteins, is a reversible mechanism and plays a critical role in eukaryotic genes activation/deactivation. Acetyltransferases are very well conserved through evolution. This allows the use of a simple model organism, such as budding yeast, for the study of their related processes and to discover specific inhibitors. Following a simple yeast-based chemogenetic approach, we have identified a novel HAT (histone acetyltransferase) inhibitor active both in vitro and in vivo. This new synthetic compound, 1-(4-(4-chlorophenyl)thiazol-2- yl)-2-(propan-2-ylidene)hydrazine, named BF1, showed substrate selectivity for histone H3 acetylation and inhibitory activity in vitro on recombinant HAT Gcn5 and p300. Finally, we tested BF1 on human cells, HeLa as control and two aggressive cancer cell lines: a neuroblastoma from neuronal tissue and glioblastoma from brain tumour. Both global acetylation of histone H3 and specific acetylation at lysine 18 (H3AcK18) were lowered by BF1 treatment. Collectively, our results show the efficacy of this novel HAT inhibitor and propose the utilization of BF1 as a new, promising tool for future pharmacological studies.