29274-35-9

Basic information

• Product Name: 5-METHYLPYRAZOLO[1,5-A]PYRIMIDIN-7(4H)-ONE
• Synonyms: 5-METHYLPYRAZOLO[1,5-A]PYRIMIDIN-7(4H)-ONE
• CAS NO: 29274-35-9
• Molecular Formula: C7H7N3O
• Molecular Weight: 149.15
• Mol File: 29274-35-9.mol
• Article Data: 7

Chemical Properties

• Appearance: /
• CAS DataBase Reference: 5-METHYLPYRAZOLO[1,5-A]PYRIMIDIN-7(4H)-ONE(CAS DataBase Reference)
• NIST Chemistry Reference: 5-METHYLPYRAZOLO[1,5-A]PYRIMIDIN-7(4H)-ONE(29274-35-9)
• EPA Substance Registry System: 5-METHYLPYRAZOLO[1,5-A]PYRIMIDIN-7(4H)-ONE(29274-35-9)

Safety Data

• Hazardous Substances Data: 29274-35-9(Hazardous Substances Data)

Upstream product

• 30414-53-0 methyl propanoyl acetate 
• 1225387-53-0 3⁽⁵⁾-aminopyrazole 
• 105-45-3 acetoacetic acid methyl ester 
• 141-97-9 ethyl acetoacetate 
• 1820-80-0 3-aminopyrazole 

Downstream Products

• 58347-47-0 3-bromo-7-chloro-5-methylpyrazolo[1,5-a]pyrimidine 

Relevant articles and documents

Structural Insights into the Inhibition of Undecaprenyl Pyrophosphate Synthase from Gram-Positive Bacteria

The polyprenyl lipid undecaprenyl phosphate (C55P) is the universal carrier lipid for the biosynthesis of bacterial cell wall polymers. C55P is synthesized in its pyrophosphate form by undecaprenyl pyrophosphate synthase (UppS), an essentialcis-prenyltransferase that is an attractive target for antibiotic development. We previously identified a compound (MAC-0547630) that showed promise as a novel class of inhibitor and an ability to potentiate β-lactam antibiotics. Here, we provide a structural model for MAC-0547630’s inhibition of UppS and a structural rationale for its enhanced effect on UppS fromBacillus subtilisversusStaphylococcus aureus. We also describe the synthesis of a MAC-0547630 derivative (JPD447), show that it too can potentiate β-lactam antibiotics, and provide a structural rationale for its improved potentiation. Finally, we present an improved structural model of clomiphene’s inhibition of UppS. Taken together, our data provide a foundation for structure-guided drug design of more potent UppS inhibitors in the future.

Development of Highly Potent, Selective, and Cellular Active Triazolo[1,5- a]pyrimidine-Based Inhibitors Targeting the DCN1-UBC12 Protein-Protein Interaction

The cullin-RING ubiquitin ligases (CRLs) are responsible for about 20% of cellular protein degradation and regulate diverse cellular processes, and the dysfunction of CRLs is implicated in human diseases. Targeting the CRLs has become an emerging strategy for the treatment of human diseases. Herein, we describe the discovery of a hit compound from our in-house library and further structure-based optimizations, which have enabled the identification of new triazolo[1,5-a]pyrimidine-based inhibitors targeting the DCN1-UBC12 interaction. Compound WS-383 blocks the DCN1-UBC12 interaction (IC50 = 11 nM) reversibly and shows selectivity over selected kinases. WS-383 exhibits cellular target engagement to DCN1 in MGC-803 cells. WS-383 inhibits Cul3/1 neddylation selectively over other cullins and also induces accumulation of p21, p27, and NRF2. Collectively, targeting the DCN1-UBC12 interaction would be a viable strategy for selective neddylation inhibition of Cul3/1 and may be of therapeutic potential for disease treatment in which Cul3/1 is dysregulated.

Discovery and characterization of a novel 7-aminopyrazolo[1,5-a]pyrimidine analog as a potent hepatitis C virus inhibitor

We describe a novel 7-aminopyrazolo[1,5-a]pyrimidine (7-APP) derivative as a potent hepatitis C virus (HCV) inhibitor. A series of 7-APPs was synthesized and evaluated for inhibitory activity against HCV in different cell culture systems. The synthesis and preliminary structure-activity relationship study of 7-APP are reported.