221243-77-2

Usage

Uses

Used in Pharmaceutical Industry:
4-Amino-1-tert-butyl-3-(1'-naphthylmethyl)-4-cyanopyrazole is used as a tyrosine kinase inhibitor for its high potency (IC50=1.5nM) and unique specificity. This makes it a valuable compound in the development of targeted therapies for various diseases, particularly those involving abnormal tyrosine kinase activity, such as certain types of cancer.
Used in Cancer Research:
In the field of cancer research, 4-Amino-1-tert-butyl-3-(1'-naphthylmethyl)-4-cyanopyrazole serves as a valuable tool for studying the role of tyrosine kinases in cancer cell growth and proliferation. Its high potency and specificity allow researchers to investigate the molecular mechanisms underlying cancer development and progression, potentially leading to the discovery of novel therapeutic strategies.
Used in Drug Development:
4-Amino-1-tert-butyl-3-(1'-naphthylmethyl)-4-cyanopyrazole is used as a lead compound in the development of new drugs targeting tyrosine kinases. Its unique properties make it an attractive starting point for the design and synthesis of more potent and selective inhibitors, which could be used in the treatment of various diseases, including cancer and other conditions characterized by dysregulated tyrosine kinase activity.

InChI:InChI=1/C19H20N4/c1-19(2,3)23-18(21)16(12-20)17(22-23)11-14-9-6-8-13-7-4-5-10-15(13)14/h4-10H,11,21H2,1-3H3

Upstream product

• 86-87-3 naphth-1-yl acetic acid 
• 32064-67-8 tert-butylhydrazine 
• 221243-13-6 2-(1-methoxy-2-naphthalen-1-ylethylidene)malononitrile 
• 5121-00-6 naphthalen-1-yl-acetyl chloride 
• 7400-27-3 tertbutylhydrazine hydrochloride 

Downstream Products

• 221244-14-0 1-tert-butyl-3-(naphthalen-1-ylmethyl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine 

Relevant academic research and scientific papers

Discovery of a potent protein kinase D inhibitor: insights in the binding mode of pyrazolo[3,4-d]pyrimidine analogues

In this study, we set out to rationally optimize PKD inhibitors based on the pyrazolo[3,4-d]pyrimidine scaffold. The lead compound for this study was 1-NM-PP1, which was previously found by us and others to inhibit PKD. In our screening we identified one compound (3-IN-PP1) displaying a 10-fold increase in potency over 1-NM-PP1, opening new possibilities for specific protein kinase inhibitors for kinases that show sensitivity towards pyrazolo[3,4-d]pyrimidine derived compounds. Interestingly the observed SAR was not in complete agreement with the commonly observed binding mode where the pyrazolo[3,4-d]pyrimidine compounds are bound in a similar fashion as PKD's natural ligand ATP. Therefore we suggest an alternate binding mode where the compounds are flipped 180 degrees. This possible alternate binding mode for pyrazolo[3,4-d]pyrimidine based compounds could pave the way for a new class of specific protein kinase inhibitors for kinases sensitive towards pyrazolo[3,4-d]pyrmidines.

Optimizing small molecule inhibitors of calcium-dependent protein kinase 1 to prevent infection by toxoplasma gondii

Toxoplasma gondii is sensitive to bulky pyrazolo [3,4-d] pyrimidine (PP) inhibitors due to the presence of a Gly gatekeeper in the essential calcium dependent protein kinase 1 (CDPK1). Here we synthesized a number of new derivatives of 3-methyl-benzyl-PP (3-MB-PP, or 1). The potency of PP analogues in inhibiting CDPK1 enzyme activity in vitro (low nM IC50 values) and blocking parasite growth in host cell monolayers in vivo (low μM EC 50 values) were highly correlated and occurred in a CDPK1-specific manner. Chemical modification of the PP scaffold to increase half-life in the presence of microsomes in vitro led to identification of compounds with enhanced stability while retaining activity. Several of these more potent compounds were able to prevent lethal infection with T. gondii in the mouse model. Collectively, the strategies outlined here provide a route for development of more effective compounds for treatment of toxoplasmosis and perhaps related parasitic diseases.

Generation of monospecific nanomolar tyrosine kinase inhibitors via a chemical genetic approach

Selective protein kinase inhibitors are highly sought after as tools for studying cellular signal transduction cascades, yet few have been discovered due to the highly conserved fold of kinase catalytic domains. Through a combination of small molecule syn