1000512-15-1

Basic information

• Product Name: (4-(aminomethyl)-2-fluorophenyl)methanol
• Synonyms: (4-(aminomethyl)-2-fluorophenyl)methanol
• CAS NO: 1000512-15-1
• Molecular Weight: 155.172
• Mol File: 1000512-15-1.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: (4-(aminomethyl)-2-fluorophenyl)methanol(CAS DataBase Reference)
• NIST Chemistry Reference: (4-(aminomethyl)-2-fluorophenyl)methanol(1000512-15-1)
• EPA Substance Registry System: (4-(aminomethyl)-2-fluorophenyl)methanol(1000512-15-1)

Safety Data

• Hazardous Substances Data: 1000512-15-1(Hazardous Substances Data)

Usage

Description

(4-(aminomethyl)-2-fluorophenyl)methanol is a chemical compound characterized by its molecular formula C9H10FNO, representing a white solid substance with a molecular weight of 157.18 g/mol. (4-(aminomethyl)-2-fluorophenyl)methanol serves as a versatile building block in the synthesis of a wide array of organic compounds, including those found in the pharmaceutical, agrochemical, and materials industries. Its utility extends to the production of specific drugs and the development of novel chemical entities, with its properties and applications varying based on the synthesis method employed.

Uses

Used in Pharmaceutical Industry:
(4-(aminomethyl)-2-fluorophenyl)methanol is used as a key intermediate for the synthesis of various pharmaceuticals, contributing to the development of new drugs and therapeutic agents. Its unique structure allows for the creation of molecules with specific biological activities, targeting a range of medical conditions.
Used in Agrochemical Industry:
In the agrochemical sector, (4-(aminomethyl)-2-fluorophenyl)methanol is utilized as a building block for the synthesis of compounds with pesticidal, herbicidal, or fungicidal properties. Its incorporation into these chemicals can enhance their effectiveness in protecting crops and improving agricultural yields.
Used in Materials Industry:
(4-(aminomethyl)-2-fluorophenyl)methanol is also employed in the materials industry, where it serves as a component in the development of advanced materials with specialized properties. These materials may find applications in various fields, such as electronics, coatings, or adhesives, due to their unique characteristics derived from the compound's structure.
Used in the Development of New Chemical Entities:
(4-(aminomethyl)-2-fluorophenyl)methanol is used as a crucial building block in the research and development of new chemical entities. Its versatility in chemical synthesis allows for the exploration of novel molecular structures with potential applications in various industries, including but not limited to pharmaceuticals, agrochemicals, and materials science.

Upstream product

• 219873-06-0 3-fluoro-4-(hydroxymethyl)benzonitrile 
• 164149-28-4 4-cyano-2-fluorobenzoic acid 

Relevant articles and documents

Discovery of Selective Small-Molecule Inhibitors for the ENL YEATS Domain

Eleven-nineteen leukemia (ENL) protein is a histone acetylation reader essential for disease maintenance in acute leukemias, in particular, the mixed-lineage leukemia (MLL)-rearranged leukemia. In this study, we carried out high-throughput screening of a small-molecule library to identify inhibitors for the ENL YEATS domain. Structure-activity relationship studies of the hits and structure-based inhibitor design led to two compounds, 11 and 24, with IC50 values below 100 nM in inhibiting the ENL-acetyl-H3 interaction. Both compounds, and their precursor compound 7, displayed strong selectivity toward the ENL YEATS domain over all other human YEATS domains. Moreover, 7 exhibited on-target inhibition of ENL in cultured cells and a synergistic effect with the bromodomain and extraterminal domain inhibitor JQ1 in killing leukemia cells. Together, we have developed selective chemical probes for the ENL YEATS domain, providing the basis for further medicinal chemistry-based optimization to advance both basic and translational research of ENL.

Selective targeting of dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (Dc-Sign) with mannose-based glycomimetics: Synthesis and interaction studies of bis(benzylamide) derivatives of a pseudomannobioside

Dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN) and Langerin are C-type lectins of dendritic cells (DCs) that share a specificity for mannose and are involved in pathogen recognition. HIV is known to use DC-SIGN on DCs to facilitate transinfection of T-cells. Langerin, on the contrary, contributes to virus elimination; therefore, the inhibition of this latter receptor is undesired. Glycomimetic molecules targeting DC-SIGN have been reported as promising agents for the inhibition of viral infections and for the modulation of immune responses mediated by DC-SIGN. We show here for the first time that glycomimetics based on a mannose anchor can be tuned to selectively inhibit DC-SIGN over Langerin. Based on structural and binding studies of a mannobioside mimic previously described by us (2), a focused library of derivatives was designed. The optimized synthesis gave fast and efficient access to a group of bis(amides), decorated with an azide-terminated tether allowing further conjugation. SPR inhibition tests showed improvements over the parent pseudomannobioside by a factor of 3-4. A dimeric, macrocyclic structure (11) was also serendipitously obtained, which afforded a 30-fold gain over the starting compound (2). The same ligands were tested against Langerin and found to exhibit high selectivity towards DC-SIGN. Structural studies using saturation transfer difference NMR spectroscopy (STD-NMR) were performed to analyze the binding mode of one representative library member with DC-SIGN. Despite the overlap of some signals, it was established that the new ligand interacts with the protein in the same fashion as the parent pseudodisaccharide. The two aromatic amide moieties showed relatively high saturation in the STD spectrum, which suggests that the improved potency of the bis(amides) over the parent dimethyl ester can be attributed to lipophilic interactions between the aromatic groups of the ligand and the binding site of DC-SIGN. Receptor targeting: For the first time glycomimetics based on a mannose anchor have been tuned to selectively inhibit DC-SIGN (dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin) over Langerin. Based on structural and binding studies of a mannobioside mimic previously described, a focused library of derivatives was designed (see figure). Copyright