221243-13-6

Basic information

• Product Name: 2-(1-METHOXY-2-(NAPHTHALEN-1-YL)ETHYLIDENE)MALONONITRILE
• Synonyms: 2-(1-METHOXY-2-(NAPHTHALEN-1-YL)ETHYLIDENE)MALONONITRILE
• CAS NO: 221243-13-6
• Molecular Formula: C₁₆H₁₂N₂O
• Molecular Weight: 248.27928
• Mol File: 221243-13-6.mol

Chemical Properties

• Appearance: /
• CAS DataBase Reference: 2-(1-METHOXY-2-(NAPHTHALEN-1-YL)ETHYLIDENE)MALONONITRILE(CAS DataBase Reference)
• NIST Chemistry Reference: 2-(1-METHOXY-2-(NAPHTHALEN-1-YL)ETHYLIDENE)MALONONITRILE(221243-13-6)
• EPA Substance Registry System: 2-(1-METHOXY-2-(NAPHTHALEN-1-YL)ETHYLIDENE)MALONONITRILE(221243-13-6)

Safety Data

• Hazardous Substances Data: 221243-13-6(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
2-(1-METHOXY-2-(NAPHTHALEN-1-YL)ETHYLIDENE)MALONONITRILE is used as an intermediate in the synthesis of 4-Amino-1-tert-butyl-3-(1’-naphthylmethyl)pyrazolo[3,4-d]pyrimidine (A603003), a highly potent and uniquely specific tyrosine kinase inhibitor. This inhibitor is designed to target a rationally engineered v-Src tyrosine kinase, which is a crucial protein in various cellular signaling pathways. By inhibiting this enzyme, A603003 can potentially disrupt the signaling pathways involved in cell proliferation, differentiation, and survival, making it a promising candidate for the development of targeted therapies against cancer and other diseases.
The application of 2-(1-METHOXY-2-(NAPHTHALEN-1-YL)ETHYLIDENE)MALONONITRILE in the pharmaceutical industry is primarily due to its ability to contribute to the development of highly specific and potent inhibitors. These inhibitors can be used to target specific proteins or enzymes involved in various diseases, leading to more effective and targeted treatments with fewer side effects. The compound's unique chemical structure allows it to be a valuable building block in the synthesis of such inhibitors, making it an essential component in the development of novel therapeutic agents.

Upstream product

• 86-87-3 naphth-1-yl acetic acid 
• 5121-00-6 naphthalen-1-yl-acetyl chloride 
• 77-78-1 dimethyl sulfate 

Downstream Products

• 221243-77-2 5-amino-1-tert-butyl-3-naphthalen-1-ylmethyl-1H-pyrazole-4-carbonitrile 
• 476371-69-4 3-naphthalen-1-ylmethyl-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine 
• 221244-14-0 1-tert-butyl-3-(naphthalen-1-ylmethyl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine 
• 476371-73-0 1-((2S,3R,4S,5R)-3,4-dibenzoyl-5-benzoylmethyltetrahydrofuran-2-yl)-3-naphthalen-1-ylmethyl-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine 

Relevant articles and documents

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.

COMPOSITIONS AND METHODS FOR TREATING TOXOPLASMOSIS. CRYPTOSPORIDIOSIS AND OTHER APICOMPLEXAN PROTOZOAN RELATED DISEASES

Compositions and methods for the treatment of toxoplasmosis-, caused by the infectious eukaryotic parasite Toxoplasma gondii (T, gondii) and for the treatment of ciyptosporidiosis, caused by the infectious eukaryotic parasites Cryptosporidium parvum (C parvuai) and Cnγtosporidium homimus (C. hominus) are described. In particular, the present disclosure is directed to compositions and methods for inhibiting either T. gondii calcium dependent protein kinases (TgCDPKs) or C. parvum and C. hominus calcium dependent protein kinases (CpDPKS) using pyrazolopyriinidine and/or imidazo[l,5-a]pyraziαe inhibitors, of the formula.(I), wherein the variables X. Y, Z, L. R1. and R3 are defined herein.

Inhibitor scaffolds as new allele specific kinase substrates

The elucidation of protein kinase signaling networks is challenging due to the large size of the protein kinase superfamily (>500 human kinases). Here we describe a new class of orthogonal triphosphate substrate analogues for the direct labeling of analog

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