94341-55-6

Usage

Uses

Used in Pharmaceutical Research:
Methanone, [4-(aminomethyl)phenyl]phenylis used as a key intermediate in the production of pharmaceuticals and other organic compounds. It plays a crucial role in the synthesis of various drugs and contributes to the development of new drug candidates.
Used in Organic Synthesis:
Methanone, [4-(aminomethyl)phenyl]phenylis used as a valuable building block in the preparation of various biological and pharmacological compounds. Its unique structure and functional groups make it an essential component in the synthesis of complex organic molecules.
Used in Drug Development:
Methanone, [4-(aminomethyl)phenyl]phenylis studied for its potential therapeutic properties, making it a promising candidate for the development of new drugs. Its unique chemical properties and interactions with biological systems offer opportunities for the discovery of novel therapeutic agents.

Upstream product

• 94341-52-3 (4-(azidomethyl)phenyl)(phenyl)methanone 
• 32752-54-8 4-(bromomethyl)benzophenone 
• 134-84-9 4-Methylbenzophenone 
• 24095-40-7 4-(aminomethyl)phenyl(phenyl)methanone hydrochloride 
• 187410-78-2 4-(N-formylaminomethyl)benzophenone 

Downstream Products

• 56431-17-5 4-aminomethyl-α-ethyl-benzhydrol 
• 1373502-22-7 N-(4-benzoylbenzyl)-6-formamidohexanamide 
• 1373502-23-8 N-(4-benzoylbenzyl)-6-isocyanohexanamide 
• 1373501-75-7 C₄₆H₄₆N₄O₈ 
• 1373501-77-9 C₄₇H₄₈N₄O₈ 
• 1373501-78-0 C₄₈H₅₀N₄O₈ 

Relevant academic research and scientific papers

SMALL MOLECULE INHIBITORS OF Id PROTEINS

The present technology relates generally to compounds, compositions, and methods useful for treating, preventing, and/or ameliorating pathogenic cellular proliferation, angiogenesis, cancer, metastatic disease, and/or a pathogenic vascular proliferative disease in a subject.

Interaction Studies between Carbonic Anhydrase and a Sulfonamide Inhibitor by Experimental and Theoretical Approaches

The most used approaches in structure-based drug design possess peculiar characteristics with advantages and limitations, and thus the management of complementary data from various techniques is of particular interest to synergistically achieve the develo

Development of a Raltegravir-based Photoaffinity-Labeled Probe for Human Immunodeficiency Virus-1 Integrase Capture

Photoaffinity labeling (PAL) is one of the upcoming and powerful tools in the field of molecular recognition. It includes the determination of dynamic parameters, such as the identification and localization of the target protein and the site of drug binding. In this study, a photoaffinity-labeled probe for full-length human immunodeficiency virus-1 integrase (HIV-1 IN) capture was designed and synthesized, following the structure of the FDA-approved drug Raltegravir. This photoprobe was found to retain the HIV IN inhibitory potential in comparison with its parent molecule and demonstrates the ability to label the HIV-1 IN protein. Putative photoprobe/inhibitor binding sites near the catalytic site were then identified after protein digestion coupled to mass and molecular modeling analyses.

ANTIBACTERIAL HYDROPHILIC COMPOUND AND USE THEREOF

The present disclosure provides an antibacterial hydrophilic compound. The antibacterial hydrophilic compound may react, induced by light through a hydrogen abstraction group in the structural formula thereof, with a C—H group and thus bind to a surface of a material having the C—H group (for example, chemical fibers such as polyester, chinlon, and the like; plastics, rubbers, and other similar materials), which can impart a durable antibacterial activity and hydrophilicity to the material. The antibacterial hydrophilic compound has a relatively strong binding force to the surface of the material without damaging the mechanical properties of the raw material. The present disclosure also provides a modified material that is modified by the antibacterial hydrophilic compound.

Antistatic compound, surface treatment method for material, and modified material

The present invention provides an antistatic compound. The antistatic compound is obtained by chemically reacting a compound with the structural formula represented by L1' or L2' with a compound Q', and the compound Q' is one or more of a polyhydroxy compound, a polycarboxy compound and a polysulfonate compound; L1' and L2' are shown in the description; and in the formulas L1' and L2', r is 1 or 2, Y is one of a single bond, the oxygen atom, the sulfur atom, the selenium atom, -C(O)-, -SO2-, -NH- and a C1-3 alkylene group, R1 to R10 and R to R are respectively independently selected from the hydrogen atom, a halogen atom, a monovalent polar group and a substituted or unsubstituted monovalent C1-18 hydrocarbon group, and at least one of the R1 to R10 or R to R reacts with the compound Q' to achieve chemical bonding. The antistatic compound can be combined with -CH- group-containing materials such as polyester and nylon to make the materials have antistatic properties and dyeability without reducing the mechanical properties of the materials.

Ugi reaction-assisted rapid assembly of affinity-based probes against potential protein tyrosine phosphatases

The multi-component Ugi reaction has been employed to assemble a small library of affinity-based probes (AfBPs) that target potential protein tyrosine phosphatases. The probes showed good labelling of PTP1B and MptpB, and were subsequently used to label endogenous PTP1B in MCF-7 cell lysates.

Structure-activity relationships in the binding of chemically derivatized CD4 to gp120 from human immunodeficiency virus

The first step in HIV infection is the binding of the envelope glycoprotein gp120 to the host cell receptor CD4. An interfacial "Phe43 cavity" in gp120, adjacent to residue Phe43 of gp120-bound CD4, has been suggested as a potential target for therapeutic intervention. We designed a CD4 mutant (D1D2F43C) for site-specific coupling of compounds for screening against the cavity. Altogether, 81 cysteine-reactive compounds were designed, synthesized, and tested. Eight derivatives exceeded the affinity of native D1D2 for gp120. Structure-activity relationships (SAR) for derivatized CD4 binding to gp120 revealed significant plasticity of the Phe43 cavity and a narrow entrance. The primary contacts for compound recognition inside the cavity were found to be van der Waals interactions, whereas hydrophilic interactions were detected in the entrance. This first SAR on ligand binding to an interior cavity of gp120 may provide a starting point for structure-based assembly of small molecules targeting gp120-CD4 interaction.

Parallel synthesis of DAPT derivatives and their γ-secretase- inhibitory activity

Parallel synthesis of the C-terminal-modified DAPT (1) derivatives was accomplished utilizing our novel resin 7. Condensation reaction of the N-acylamino acid 10 with the amines 11a-o proceeded smoothly to give the corresponding amides 6a-o without any epimerization. Among the analogues, the benzophenonemethyl amide derivative 6o showed 30 times more potent activity than the original DAPT (1).

Radiation-curable compositions containing photoinitiators linked by a covalent bond

A process for the preparation of a radiation-curable acrylate composition, wherein to compounds A containing at least 2 acrylic groups there are added benzophenone derivatives which are not copolymerizable by free-radical copolymerization and which contain at least one primary or secondary amino group or a hydroxyl group or a mercapto group.

Photoaffinity labeling of rat steroid 5α-reductase (isozyme-1) by a benzophenone derivative of a 4-methyl-4-azasteroid

[1,2-3H]N-4(Benzylbenzoyl)-3-oxo-4-aza-4-methyl-5α-androstane-17β- carboxamide ([3H]-4MABP) has been synthesized as a photoaffinity probe of the steroid 5α-reductase isozyme-1 (5αR-1). Reversible binding of the probe to 5αR-1 in microsomal preparations yielded a reversible dissociation constant (K(d)) of ~3 nM, whereas inhibition experiments indicated that the probe had a 50% inhibition concentration of 4.4 nM and was a competitive inhibitor of the enzyme (K(i) ? 3 nM) with respect to testosterone. SDS- PAGE analysis of microsomal, detergent-solubilized, and (6.5%) polyethylene glycol-precipitated fractions of 5αR-1 photolyzed with [3H]4MABP in the presence of NADPH showed that the radioactivity was incorporated into a single protein band with a mass of 26 kDa (apparent molecular weight of 5αR- 1). UV photolysis was accompanied by an irreversible loss in enzyme activity, consistent with its covalent modification. Increasing the time of UV irradiation and concentration of [3H]4MABP indicated that the half-life and apparent K(d) for its photo insertion were ~3 min and 7.5 nM, respectively. Photolysis in the presence of a 20-fold excess of N,N-diethyl-4-aza-4- methyl-3-oxo-5α-androstune-17β-carboxamide or the 3-carboxysteroid SKF- 105111 resulted in partial protection of 5αR-1 from the probe, whereas minimal incorporation of radioactivity was observed in the absence of NADPH or in the presence of NADP+. The results indicated that [3H]4MABP is an effective probe of the steroid (D-ring) binding domain of 5αR-1.