29263-67-0

Basic information

• Product Name: 2-Pyridinemethanol, a-(4-methylphenyl)-
• CAS NO: 29263-67-0
• Molecular Formula: C13H13NO
• Molecular Weight: 199.252
• Mol File: 29263-67-0.mol
• Article Data: 16

Chemical Properties

• CAS DataBase Reference: 2-Pyridinemethanol, a-(4-methylphenyl)-(CAS DataBase Reference)
• NIST Chemistry Reference: 2-Pyridinemethanol, a-(4-methylphenyl)-(29263-67-0)
• EPA Substance Registry System: 2-Pyridinemethanol, a-(4-methylphenyl)-(29263-67-0)

Safety Data

• Hazardous Substances Data: 29263-67-0(Hazardous Substances Data)

Upstream product

• 29335-87-3 2-(4-methyl-benzyl)-pyridine 
• 67-68-5 dimethyl sulfoxide 
• 78539-88-5 2-(4-toluoyl)pyridine 
• 106-38-7 para-bromotoluene 
• 100-70-9 2-Cyanopyridine 
• 1121-60-4 pyridine-2-carbaldehyde 
• 108-88-3 toluene 
• 109-04-6 2-bromo-pyridine 
• 104-87-0 4-methyl-benzaldehyde 
• 4294-57-9 para-methylphenylmagnesium bromide 
• 21970-13-8 (pyridin-2-yl)magnesium bromide 
• 98-98-6 2-Picolinic acid 

Downstream Products

• 78539-88-5 2-(4-toluoyl)pyridine 
• 1353686-69-7 C₁₅H₁₃NO 
• 1353686-75-5 8a-(p-tolyl)indolizinone 
• 1353686-80-2 C₁₅H₁₇NO 
• 109810-35-7 phenyl(pyridin-2-yl)(p-tolyl)methanol 
• 59742-89-1 3-(4-methylphenyl)-[1,2,3]triazolo[1,5-a]pyridine 
• 59742-92-6 2-pyridyl 4-tolyl ketone hydrazone 
• 782504-65-8 2-[(4-methylphenyl)methyl]piperidine hydrochloride 
• 75343-78-1 Piperidin-2-yl-p-tolyl-methanol 
• 75343-78-1 Piperidin-2-yl-p-tolyl-methanol 
• 29335-87-3 2-(4-methyl-benzyl)-pyridine 

Relevant articles and documents

Green synthesis method of polyaryl substituted methanol

The invention relates to a green synthesis method of polyaryl substituted methanol, in particular to a method for efficiently synthesizing polyaryl substituted methanol in a polar aprotic solvent under the condition of an oxidizing agent by taking polyaryl substituted methane as a raw material and alkali as an additive. The method provided by the invention is green and environment-friendly, avoids using expensive metal catalysts, and has the advantages of low cost, few reaction steps, short time, high yield and the like.

Targeting the aryl hydrocarbon receptor with a novel set of triarylmethanes

The aryl hydrocarbon receptor (AhR) is a chemical sensor upregulating the transcription of responsive genes associated with endocrine homeostasis, oxidative balance and diverse metabolic, immunological and inflammatory processes, which have raised the pharmacological interest on its modulation. Herein, a novel set of 32 unsymmetrical triarylmethane (TAM) class of structures has been synthesized, characterized and their AhR transcriptional activity evaluated using a cell-based assay. Eight of the assayed TAM compounds (14, 15, 18, 19, 21, 22, 25, 28) exhibited AhR agonism but none of them showed antagonist effects. TAMs bearing benzotrifluoride, naphthol or heteroaromatic (indole, quinoline or thiophene) rings seem to be prone to AhR activation unlike phenyl substituted or benzotriazole derivatives. A molecular docking analysis with the AhR ligand binding domain (LBD) showed similarities in the binding mode and in the interactions of the most potent TAM identified 4-(pyridin-2-yl (thiophen-2-yl)methyl)phenol (22) compared to the endogenous AhR agonist 5,11-dihydroindolo[3,2-b]carbazole-12-carbaldehyde (FICZ). Finally, in silico predictions of physicochemical and biopharmaceutical properties for the most potent agonistic compounds were performed and these exhibited acceptable druglikeness and good ADME profiles. To our knowledge, this is the first study assessing the AhR modulatory effects of unsymmetrical TAM class of compounds.

Conformational Dynamics-Guided Loop Engineering of an Alcohol Dehydrogenase: Capture, Turnover and Enantioselective Transformation of Difficult-to-Reduce Ketones

Directed evolution of enzymes for the asymmetric reduction of prochiral ketones to produce enantio-pure secondary alcohols is particularly attractive in organic synthesis. Loops located at the active pocket of enzymes often participate in conformational changes required to fine-tune residues for substrate binding and catalysis. It is therefore of great interest to control the substrate specificity and stereochemistry of enzymatic reactions by manipulating the conformational dynamics. Herein, a secondary alcohol dehydrogenase was chosen to enantioselectively catalyze the transformation of difficult-to-reduce bulky ketones, which are not accepted by the wildtype enzyme. Guided by previous work and particularly by structural analysis and molecular dynamics (MD) simulations, two key residues alanine 85 (A85) and isoleucine 86 (I86) situated at the binding pocket were thought to increase the fluctuation of a loop region, thereby yielding a larger volume of the binding pocket to accommodate bulky substrates. Subsequently, site-directed saturation mutagenesis was performed at the two sites. The best mutant, where residue alanine 85 was mutated to glycine and isoleucine 86 to leucine (A85G/I86L), can efficiently reduce bulky ketones to the corresponding pharmaceutically interesting alcohols with high enantioselectivities (～99% ee). Taken together, this study demonstrates that introducing appropriate mutations at key residues can induce a higher flexibility of the active site loop, resulting in the improvement of substrate specificity and enantioselectivity. (Figure presented.).