1255099-09-2

Basic information

• Product Name: 1-tert-butyl 4-ethyl 4-(trifluoromethyl)piperidine-1,4-dicarboxylate
• Synonyms: 1-tert-butyl 4-ethyl 4-(trifluoromethyl)piperidine-1,4-dicarboxylate
• CAS NO: 1255099-09-2
• Molecular Formula: C14H23F3NO4
• Molecular Weight: 326.3319296
• Mol File: 1255099-09-2.mol
• Article Data: 4

Chemical Properties

• Appearance: /
• CAS DataBase Reference: 1-tert-butyl 4-ethyl 4-(trifluoromethyl)piperidine-1,4-dicarboxylate(CAS DataBase Reference)
• NIST Chemistry Reference: 1-tert-butyl 4-ethyl 4-(trifluoromethyl)piperidine-1,4-dicarboxylate(1255099-09-2)
• EPA Substance Registry System: 1-tert-butyl 4-ethyl 4-(trifluoromethyl)piperidine-1,4-dicarboxylate(1255099-09-2)

Safety Data

• Hazardous Substances Data: 1255099-09-2(Hazardous Substances Data)

Usage

Chemical class

piperidine derivatives

Type of compound

ester

Structural components

piperidine ring, tert-butyl, ethyl, and trifluoromethyl substituents, carboxylate groups at the 1 and 4 positions

Potential applications

medicinal and pharmaceutical research

Possible uses

building block for synthesis of novel drug candidates, reference standard in analytical chemistry

Variability

specific properties and potential uses may vary depending on context and research or development goals

Upstream product

• 142851-03-4 1-tert-butyl 4-ethyl piperidine-1,4-dicarboxylate 
• 129946-88-9 Umemoto's reagent 

Downstream Products

• 495415-51-5 1-(tert-butoxycarbonyl)-4-(trifluoromethyl)piperidine-4-carboxylic acid 

Relevant articles and documents

Protein Modification at Tyrosine with Iminoxyl Radicals

Post-translational modifications (PTMs) of proteins are a biological mechanism for reversibly controlling protein function. Synthetic protein modifications (SPMs) at specific canonical amino acids can mimic PTMs. However, reversible SPMs at hydrophobic amino acid residues in proteins are especially limited. Here, we report a tyrosine (Tyr)-selective SPM utilizing persistent iminoxyl radicals, which are readily generated from sterically hindered oximes via single-electron oxidation. The reactivity of iminoxyl radicals with Tyr was dependent on the steric and electronic demands of oximes; isopropyl methyl piperidinium oxime 1f formed stable adducts, whereas the reaction of tert-butyl methyl piperidinium oxime 1o was reversible. The difference in reversibility between 1f and 1o, differentiated only by one methyl group, is due to the stability of iminoxyl radicals, which is partly dictated by the bond dissociation energy of oxime O-H groups. The Tyr-selective modifications with 1f and 1o proceeded under physiologically relevant, mild conditions. Specifically, the stable Tyr-modification with 1f introduced functional small molecules, including an azobenzene photoswitch, to proteins. Moreover, masking critical Tyr residues by SPM with 1o, and subsequent deconjugation triggered by the treatment with a thiol, enabled on-demand control of protein functions. We applied this reversible Tyr modification with 1o to alter an enzymatic activity and the binding affinity of a monoclonal antibody with an antigen upon modification/deconjugation. The on-demand ON/OFF switch of protein functions through Tyr-selective and reversible covalent-bond formation will provide unique opportunities in biological research and therapeutics.

ANTIBACTERIAL COMPOUNDS

The present invention provides a compound of the following formula and salts thereof: Also provided is the use of these compounds as antibacterials, compositions comprising them and processes for their manufacture.