1200-05-1

Usage

Uses

Used in Pharmaceutical Synthesis:
4-AMINOMETHYLPHENYLACETIC ACID is used as a starting material for the synthesis of various pharmaceuticals, including non-steroidal anti-inflammatory drugs (NSAIDs) and antihistamines. Its presence in these medications is crucial for their therapeutic effects, such as reducing inflammation and alleviating allergic reactions.
Used in Neurological Disorder Treatment:
In the medical field, 4-AMINOMETHYLPHENYLACETIC ACID is studied for its potential applications in the treatment of neurological disorders. Its unique structure allows it to interact with specific biological targets, offering a promising avenue for the development of new therapies to address unmet medical needs.
Used in Antibiotic and Antimicrobial Agent Synthesis:
4-AMINOMETHYLPHENYLACETIC ACID is also identified as a potential precursor for the synthesis of new antibiotics and antimicrobial agents. Given the increasing prevalence of antibiotic resistance, the development of novel antimicrobial compounds is of critical importance, and 4-AMPA may play a significant role in this endeavor.
Used in Organic Compound Synthesis:
In the realm of organic chemistry, 4-AMINOMETHYLPHENYLACETIC ACID is utilized as a precursor for the synthesis of other organic compounds. Its functional groups enable a range of chemical reactions, making it a valuable building block for the creation of diverse chemical entities with potential applications across various industries.

InChI:InChI=1/C9H11NO2/c10-6-8-3-1-7(2-4-8)5-9(11)12/h1-4H,5-6,10H2,(H,11,12)

Upstream product

• 13737-36-5 4-bromophenylacetic acid 
• 5462-71-5 4-cyanophenylacetic acid 
• 103-82-2 phenylacetic acid 
• 62910-48-9 ethyl 2-[4-(aminomethyl)phenyl]acetate 
• 117885-63-9 {4-[(2-chloro-acetylamino)-methyl]-phenyl}-acetic acid 
• 109093-38-1 (4-phthalimidomethyl-phenyl)-acetic acid 
• 56066-91-2 4-chloromethylphenylacetic acid 
• 71420-92-3 2-(4-(((tert-butoxycarbonyl)amino)methyl)phenyl)acetic acid 
• 1528-41-2 ethyl 4-cyanophenylacetate 

Downstream Products

• 176504-01-1 N-(9-fluorenylmethyloxycarbonyl)-4-(aminomethyl)phenylacetic acid 
• 444807-46-9 2-(4-(aminomethyl)phenyl)acetic acid methyl ester 
• 143774-32-7 2-<4-(aminomethyl)phenyl>-5-hexynoic acid 
• 143774-33-8 2-<4-(guanidinomethyl)phenyl>-5-hexynoic acid 
• 143774-31-6 2-<4-<<<(tert-butyloxy)carbonyl>amino>methyl>phenyl>-5-hexynoic acid 
• 1610413-97-2 C₃₄H₅₄N₄O₁₀ 
• 1610414-00-0 C₃₃H₄₅N₇O₁₇S 
• 1622386-69-9 C₂₁H₁₉ClN₄O₂ 
• 1257585-83-3 C₁₅H₁₆N₄O₃S 
• 1257585-82-2 C₁₆H₁₆N₂O₄S 
• 1257585-81-1 C₉H₁₂N₂O*ClH 
• 1257585-80-0 C₁₄H₂₀N₂O₃ 

Relevant academic research and scientific papers

A new strategy applied to the synthesis of an α-helical bicyclic peptide constrained by two overlapping i, i+7 side-chain bridges of novel design

A conformationally constrained, bicyclic, 14-residue peptide containing two overlapping i, i+7 side-chain bridges has been synthesized. The design of the side-chain linkage, which is built around a p-substituted benzene ring for rigidity, and the solid-phase approach applied to the peptide synthesis, are both new. A Boc/Benzyl peptide chain assembly method was combined with Fmoc/OFm orthogonal side-chain deprotection and solid-phase cyclization to form the first side-chain lactam bridge. A 2-(2-pyridyl)ethyl group (2-Pet), activated by methylation with CH3I in DMF, was then used in combination with Fmoc to allow a second orthogonal side-chain deprotection and solid-phase cyclization to form the second bridge. The circular dichroism spectrum of the product indicates that it is highly helical.

METHODS OF TREATING CANCER WITH A PSMA LIGAND-TUBULYSIN COMPOUND

The invention described herein pertains to drug delivery conjugates for targeted therapy. The invention described herein relates to methods of treating PSMA expressing cancers with a PSMA ligand-tubulysin compound. The invention described herein also relates to methods of treating PSMA-expressing cancers with a PSMA ligand-tubulysin compound in patients where stable disease results after treatment with the PSMA ligand-tubulysin compound.

HETEROARYL-CARBOXYLIC ACIDS AS HISTONE DEMETHYLASE INHIBITORS

The invention relates to heteroaryl-carboxylic acids as described herein, useful as histone demethylase inhibitors. The invention also relates to pharmaceutical compositions comprising these compounds and to their use in therapy, including e.g., in the treatment of cancer.

METHODS OF TREATING CANCER WITH A PSMA LIGAND-TUBULYSIN COMPOUND

The invention described herein pertains to drug delivery conjugates for targeted therapy. The invention described herein relates to methods of treating PSMA expressing cancers with a PSMA ligand-tubulysin compound. The invention described herein also relates to methods of treating PSMA-expressing cancers with a PSMA ligand-tubulysin compound in patients where stable disease results after treatment with the PSMA ligand-tubulysin compound.

CONJUGATES FOR TREATING DISEASES CAUSED BY PSMA EXPRESSING CELLS

The invention described herein pertains to the diagnosis, imaging, and/or treatment of pathogenic cell populations. In particular, the invention described herein pertains to the diagnosis, imaging, and/or treatment of diseases caused by PSMA expressing cells, such as prostate cancer cells, using compounds capable of targeting PSMA expressing cells.

HETEROCYCLIC COMPOUND AND HEMATOPOIETIC STEM CELL AMPLIFIER

An expansion agent for hematopoietic stem cells and/or hematopoietic progenitor cells useful for improvement in the efficiency of gene transfer into hematopoietic stem cells for gene therapy useful for treatment of various disorders is provided. An expansion agent for hematopoietic stem cells and/or hematopoietic progenitor cells containing a compound represented by the formula (I) (wherein X, Y, Z, Ar1, R1, R2, R3, R4, R5, R6 and R7 are as defined in the description), a tautomer, prodrug or pharmaceutically acceptable salt of the compound or a solvate thereof, which can expand hematopoietic stem cells and/or hematopoietic progenitor cells.

Exploring the Sn binding pockets in gingipains by newly developed inhibitors: Structure-based design, chemistry, and activity

Arg-gingipains (Rgps) and Lys-gingipain (Kgp) are cysteine proteinases secreted by Porphyromonas gingivalis, the major pathogen implicated in periodontal disease. Gingipains are essential to the bacterium for its virulence and survival, and development of inhibitors targeting these proteins provides an approach to treat periodontal diseases. Here, we present the first example of structure-based design of gingipains inhibitors, with the use of the crystal structure of RgpB and the homology model of Kgp. Chloromethyl ketones were selected as suitable compounds to explore the specificity of the Sn binding region of both enzymes. Three series of inhibitors bearing Arg or Lys at P1 and different substituents at P2 and P3 were designed, synthesized, and tested. High potency (kobs/[I] ～ 107 M-1 s -1) was achieved for small ligands, such as the dipeptide analogues. The detailed analysis of Sn binding pockets revealed the molecular basis of inhibitory affinity and provided insight into the structure-activity relationship.

Effect of Conformational Mobility and Hydrogen-Bonding Interactions on the Selectivity of Some Guanidinoaryl-Substituted Mechanism-Based Inhibitors of Trypsin-like Serine Proteases

Previously, we had reported that some guanidino-substituted α- and β-aryl enol lactones I and II behaved as selective, mechanism-based inhibitors of some trypsin-like proteases (Rai, R.; Katzenellenbogen.J.A.J.Med.Chem., submitted).In this study, we describe the synthesis and kinetic evaluation of some related, guanidino-substituted enol lactones having greater conformational mobility and affording additional hydrogen-bonding sites at the active site.The α-aryl-substituted lactones 1 and 2, which have greater conformational mobility in the guanidinoaryl linkage than I, selectively inhibited the trypsin-like enzymes, and they were relatively poor inactivators of α-chymotrypsin and human neutrophil elastase (HNE).The iodo enol lactone 2 permanently inactivated trypsin, urokinase, tissue plasminogen activator, and plasmin, showing exceptionally high specificity in its interaction with trypsin and urokinase.The selectivity pattern exhibited by the closely related, conformationally less mobile α-aryl-substituted iodo lactone Ib, which was previously shown to be a selective suicide substrate of urokinase and plasmin, provides an interesting comparison.The α-benzamido-substituted lactones 3 and 4, which afford an additional site for active-site hydrogen bonding, were found to be very potent alternate substrate inhibitors of trypsin and urokinase.In addition, the iodo lactone 4 permanently inactivated α-chymotropsin.The importance of secondary interactions in increasing the specificities in the case of α-chymotrypsin is discussed.