304895-22-5

Basic information

• Product Name: 2-CHLORO-N-[5-(4-METHOXYBENZYL)-1,3-THIAZOL-2-YL]ACETAMIDE
• Synonyms: 2-CHLORO-N-[5-(4-METHOXYBENZYL)-1,3-THIAZOL-2-YL]ACETAMIDE
• CAS NO: 304895-22-5
• Molecular Formula: C13H13ClN2O2S
• Molecular Weight: 296.77252
• Mol File: 304895-22-5.mol

Chemical Properties

• Appearance: /
• Density: 1.348±0.06 g/cm3(Predicted)
• PKA: 7.22±0.50(Predicted)
• CAS DataBase Reference: 2-CHLORO-N-[5-(4-METHOXYBENZYL)-1,3-THIAZOL-2-YL]ACETAMIDE(CAS DataBase Reference)
• NIST Chemistry Reference: 2-CHLORO-N-[5-(4-METHOXYBENZYL)-1,3-THIAZOL-2-YL]ACETAMIDE(304895-22-5)
• EPA Substance Registry System: 2-CHLORO-N-[5-(4-METHOXYBENZYL)-1,3-THIAZOL-2-YL]ACETAMIDE(304895-22-5)

Safety Data

• Hazardous Substances Data: 304895-22-5(Hazardous Substances Data)

Upstream product

• 807667-27-2 2-chloro-3-(4-methoxyphenyl)propanal 
• 4346-59-2 para-methoxyphenyldiazonium chloride 
• 104-94-9 4-methoxy-aniline 
• 79-04-9 chloroacetyl chloride 
• 299953-06-3 5-[(4-methoxyphenyl)methyl]thiazol-2-amine 

Relevant articles and documents

Synthesis and antitumor activities of new n-(5-benzylthiazol-2-yl)-2-(heteryl-5-ylsulfanyl)-acetamides

Aim. Synthesis of a series of new N-(5-benzyl-thiazol-2-yl)-2-(heteryl-5-ylsulfanyl)-acetamides and study of their anticancer activity. Methods. Organic synthesis, analytical and spectral methods, pharmacological screening. Results. [2-chloro-N-(5-aryl-1,

Aminothiazoles as Potent and Selective Sirt2 Inhibitors: A Structure-Activity Relationship Study

Sirtuins are NAD+-dependent protein deacylases that cleave off acetyl but also other acyl groups from the ε-amino group of lysines in histones and other substrate proteins. Dysregulation of human Sirt2 (hSirt2) activity has been associated with the pathogenesis of cancer, inflammation, and neurodegeneration, which makes the modulation of hSirt2 activity a promising strategy for pharmaceutical intervention. The sirtuin rearranging ligands (SirReals) have recently been discovered by us as highly potent and isotype-selective hSirt2 inhibitors. Here, we present a well-defined structure-activity relationship study, which rationalizes the unique features of the SirReals and probes the limits of modifications on this scaffold regarding inhibitor potency. Moreover, we present a crystal structure of hSirt2 in complex with an optimized SirReal derivative that exhibits an improved in vitro activity. Lastly, we show cellular hyperacetylation of the hSirt2 targeted tubulin caused by our improved lead structure.