1822572-30-4

Basic information

• Product Name: 4-(methoxymethylcarbamoyl)-2,2-dimethyloxazolidine-3-carboxylic acid tert-butyl ester
• CAS NO: 1822572-30-4
• Molecular Weight: 288.344
• Mol File: 1822572-30-4.mol

Chemical Properties

• CAS DataBase Reference: 4-(methoxymethylcarbamoyl)-2,2-dimethyloxazolidine-3-carboxylic acid tert-butyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: 4-(methoxymethylcarbamoyl)-2,2-dimethyloxazolidine-3-carboxylic acid tert-butyl ester(1822572-30-4)
• EPA Substance Registry System: 4-(methoxymethylcarbamoyl)-2,2-dimethyloxazolidine-3-carboxylic acid tert-butyl ester(1822572-30-4)

Safety Data

• Hazardous Substances Data: 1822572-30-4(Hazardous Substances Data)

Upstream product

• 3262-72-4 (R)-N-tert-butoxycarbonyl serine 
• 209905-48-6 [2-hydroxy-1-(methoxymethylcarbamoyl)ethyl]carbamic acid tert-butyl ester 
• 77-76-9 2,2-dimethoxy-propane 
• 3850-40-6 N-Boc-DL-serine 
• 24424-99-5 di-tert-butyl dicarbonate 
• 660852-86-8 (4R)-3-(tert-butoxycarbonyl)-2,2-dimethyl-1,3-oxazolidine-4-carboxylic acid 
• 6638-79-5 N,O-dimethylhydroxylamine*hydrochloride 
• 67-64-1 acetone 
• 167102-61-6 tert-butyl N-[(1R)-1-(hydroxymethyl)-2-[methoxy(methyl)amino]-2-oxo-ethyl]carbamate 
• 108149-60-6 methyl [(4R)-3-(tert-butoxycarbonyl)-2,2-dimethyl-1,3-oxazolidin-4-yl]carboxylate 
• 95715-85-8 2-(tert-butoxycarbonylamino)-3-hydroxypropionic acid methyl ester 
• 59524-02-6 N-tert-butoxycarbonyl-L-serine benzyl ester 
• 122709-20-0 N-(tert-butoxycarbonyl)-L-serine N'-methoxy-N'-methylamide 
• 3262-72-4 (S)-N-(tert-butoxycarbonyl)serine 

Downstream Products

• 175696-50-1 tert-butyl [(2S,3S,4R)-1,3,4-trihydroxyoctadecan-2-yl]carbamate 
• 102308-32-7 (4S)-4-formyl-2,2-dimethyl-oxazolidine-3-carboxylic acid tert-butyl ester 

Relevant articles and documents

Copper mediated cyclization of 1-substituted enamides, dienamides and trienamides: regiochemistry, indigoid formation and methyl migration-aromatization

Copper mediated cyclization of activated 1-substituted enamides occurs via a 5-endo radical-polar crossover process. Trichloroacetyl derivatives can undergo further reactions post cyclization (elimination of HCl or dimerization potentially via copper carb

Direct Synthesis of N -Protected Serine- And Threonine-Derived Weinreb Amides via Diboronic Acid Anhydride-Catalyzed Dehydrative Amidation: Application to the Concise Synthesis of -Garner's Aldehyde

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C10-ALKYLENE SUBSTITUTED 13-MEMBERED MACROLIDES AND USES THEREOF

Provided are 13-membered macrolides for the treatment of infectious diseases. The 13-membered macrolides described herein are azaketolides. Also provided are methods for preparing the 13- membered macrolides, pharmaceutical compositions comprising the 13-membered macrolides, and methods of treating infectious diseases, and in particular, disease resulting from Gram negative bacteria using the disclosed macrolides. Formula (I)

STABLE N-((1R,2R)-1-(2,3-DIHYDROBENZO[B][1,4]DIOXIN-6-YL)-1-HYDROXY-3-(PYRROLIDIN-1-YL)PROPAN-2-YL) OCTANAMIDE (2R,3R)-2,3-DIHYDROXYSUCCINATE PREMIX AND PROCESS FOR PREPARATION THEREOF

The present invention related to stable N-((1R, 2R)-1-(2,3-dihydrobenzo[b][1,4] dioxin-6-yl)- 1-hydroxy-3- (pyrrolidin-1-yl)propan-2-yl) octanamide (2R,3R)- 2,3-dihydroxysuccinate premix of formula (Ia) and its process for preparation thereof. The present invention also related to process for the preparation of N-((1R, 2R)-1-(2,3-dihydrobenzo[b][1,4] dioxin-6- yl)-1-hydroxy-3- (pyrrolidin-1-yl) propan-2-yl) octanamide of formula (I) and pharmaceutically acceptable salts.

DEUTERATED O-SULFATED BETA-LACTAM HYDROXAMIC ACIDS AND DEUTERATED N-SULFATED BETA-LACTAMS

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Novel Easily Recyclable Bifunctional Phosphonic Acid Carrying Tripeptides for the Stereoselective Michael Addition of Aldehydes with Nitroalkenes

A novel bifunctional organocatalyst library combining both aminocatalysis and phosphonic acid activation was used for the first time as an efficient tool for the stereoselective Michael addition of aldehydes with several aromatic nitroalkenes with good selectivities up to 95:5 dr and 93:7 er. Due to their high water solubility, the catalysts were easily recyclable and could be reused over several cycles without any significant loss of selectivity.

Protein and peptide-free synthetic vaccines against streptococcus pneumoniae type 3

The present invention provides a protein- and peptide-free conjugate comprising a synthetic carbohydrate and a carrier molecule, wherein the synthetic carbohydrate is a Streptococcus pneumoniae type 3 capsular polysaccharide related carbohydrate and the carrier molecule is a glycosphingolipid. Said conjugate and pharmaceutical composition thereof are useful for immunization against diseases associated with Streptococcus pneumoniae, and more specifically against diseases associated with Streptococcus pneumoniae type 3.

PROTEIN AND PEPTIDE-FREE SYNTHETIC VACCINES AGAINST STREPTOCOCCUS PNEUMONIAE TYPE 3

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CARBOHYDRATE-GLYCOLIPID CONJUGATE VACCINES

The present invention relates to the field of synthesizing and biologically evaluating of a novel class of carbohydrate-based vaccines. The new vaccines consist of a multi-modular structure which allows applying the vaccine to a whole variety of pathogenes. This method allows preparing vaccines against all pathogens expressing immunogenic carbohydrate antigens. As conjugation of antigenic carbohydrates to proteins is not required the conjugate vaccine is particularly heat stable. No refrigeration is required, a major drawback of protein-based vaccines.

POLYSACCHARIDE ANTIGEN-GLYCOLIPID CONJUGATE VACCINES

The present invention relates to the field of synthesizing and biologically evaluating of a novel class of carbohydrate-based vaccines. The new vaccines consist of a multi-modular structure which allows applying the vaccine to a whole variety of pathogenes. This method allows preparing vaccines against all pathogens expressing immunogenic carbohydrate antigens. As conjugation of antigenic carbohydrates to proteins is not required the conjugate vaccine is particularly heat stable. No refrigeration is required, a major drawback of protein-based vaccines.