653604-38-7

Usage

Uses

Used in Organic Synthesis:
Benzenamine, 3-(cyclopentyloxy)(9CI) is used as a building block in organic synthesis for the creation of various complex organic molecules. Its unique structure allows for versatile chemical reactions, making it a valuable component in the synthesis of pharmaceuticals, agrochemicals, and other specialty chemicals.
Used in Chemical Reactions:
As a reagent, Benzenamine, 3-(cyclopentyloxy)(9CI) is utilized in a range of chemical reactions to facilitate the formation of desired products. Its presence can enhance reaction rates, improve yields, or enable specific transformations that are otherwise challenging to achieve.
Used in Pharmaceutical Industry:
Benzenamine, 3-(cyclopentyloxy)(9CI) may have potential applications in the pharmaceutical industry, although further research and testing are needed to determine its specific uses and properties. Its unique structure could contribute to the development of new drugs or drug candidates with novel therapeutic effects.
Used in Agricultural Industry:
Similarly, Benzenamine, 3-(cyclopentyloxy)(9CI) may also find applications in the agricultural industry, where it could be used in the development of new agrochemicals or as a component in the synthesis of existing ones. Further research is required to explore its potential in this field and to understand its impact on crop protection and enhancement.

InChI:InChI=1/C11H15NO/c12-9-4-3-7-11(8-9)13-10-5-1-2-6-10/h3-4,7-8,10H,1-2,5-6,12H2

Upstream product

• 1031442-10-0 1‐(cyclopentyloxy)‐3‐nitrobenzene 
• 96-41-3 Cyclopentanol 
• 591-27-5 m-Hydroxyaniline 

Downstream Products

• 653605-00-6 6-[N-(3-cyclopentyloxyphenyl)carbamyl]-2-naphthalenecarbonitrile 
• 1067239-48-8 C₁₄H₁₇ClN₂O₃ 
• 1067239-61-5 1-[3-(cyclopentyloxy)phenyl]-3-ethylurea 
• 1043931-95-8 1-(2-chloroethyl)-3-(3-(cyclopentyloxy)phenyl)urea 
• 133040-78-5 2-[2-(5-Bromo-1H-indol-3-yl)-ethyl]-3-(3-cyclopentyloxy-phenyl)-3H-quinazolin-4-one 

Relevant academic research and scientific papers

DIARYLUREAS AS CB1 ALLOSTERIC MODULATORS

The present invention provides novel diarylurea derivatives (compounds of formula (I)) and their uses. The compounds of the present invention are demonstrated to be allosteric modulators of the CB1 receptor, and therefore useful for the treatment of diseases and conditions mediated by CB1.

Cycloalkyl-substituted aryl chloroethylureas inhibiting cell cycle progression in G0/G1 phase and thioredoxin-1 nuclear translocation

1-(2-Chloroethyl)-3-(4-cyclohexylphenyl)urea (cHCEU) has been shown to abrogate the presence of thioredoxin-1 into the nucleus through its selective covalent alkylation. In the present letter we have evaluated the structure-activity relationships of the s

THERAPEUTIC COMPOUNDS

This invention relates to a novel class of substituted amino-ethoxy benzene derivatives of formula (I) which are inhibitors of serine proteases and to their use in treating aberrant serine protease activity in a mammal, contraception, anti-coagulant methods and methods for treating aberrant cell proliferation, tumours, cancer, angiogenesis, angiogenesis-based retinopathies, autoimmummune disease, inflammation, skin disease, arthritis, rheutmatoid arthritis, asthma, osteoarthritis and multiple sclerosis. (I), Wherein Rm, Rn, Rp, Rq, V, W, X, Y and R8 are as defined in the claims.

PYRIMIDINE AND QUINOLINE POTENTIATORS OF METABOTROPIC GLUTAMATE RECEPTORS

The present invention is directed to compounds which are potentiators of metabotropic glutamate receptors, including the mGluR2 receptor, and which are useful in the treatment or prevention of neurological and psychiatric disorders associated with glutama

Identification of Novel Binding Interactions in the Development of Potent, Selective 2-Naphthamidine Inhibitors of Urokinase. Synthesis, Structural Analysis, and SAR of N-Phenyl Amide 6-Substitution

The preparation and assessment of biological activity of 6-substituted 2-naphthamidine inhibitors of the serine protease urokinase plasminogen activator (uPA, or urokinase) is described. 2-Naphthamidine was chosen as a starting point based on synthetic considerations and on modeling of substituent vectors. Phenyl amides at the 6-position were found to improve binding; replacement of the amide with other two-atom linkers proved ineffective. The phenyl group itself is situated near the S1′ subsite; substitutions off of the phenyl group accessed S1′ and other distant binding regions. Three new points of interaction were defined and explored through ring substitution. A solvent-exposed salt bridge with the Asp60A carboxylate was formed using a 4-alkylamino group, improving affinity to Ki = 40 nM. Inhibitors also accessed two hydrophobic regions. One interaction is characterized by a tight hydrophobic fit made with a small dimple largely defined by His57 and His99; a weaker, less specific interaction involves alkyl groups reaching into the broad prime-side protein binding region near Val41 and the Cys42-Cys58 disulfide, displacing water molecules and leading to small gains in activity. Many inhibitors accessed two of these three regions. Affinities range as low as Ki = 6 nM, and many compounds had Ki 100 nM, while moderate to excellent selectivity was gained versus four of five members of a panel of relevant serine proteases. Also, some selectivity against trypsin was generated via the interaction with Asp60A. X-ray structures of many of these compounds were used to inform our inhibitor design and to increase our understanding of key interactions. In combination with our exploration of 8-substitution patterns, we have identified a number of novel binding interactions for uPA inhibitors.