110230-64-3

Upstream product

• 2612-30-8 2-benzyl-1,3-propanediol 
• 75-36-5 acetyl chloride 
• 49769-78-0 2-benzyl-malonic acid dimethyl ester 
• 607-81-8 diethyl 2-benzylmalonate 
• 108-05-4 vinyl acetate 
• 108-24-7 acetic anhydride 
• 100-39-0 benzyl bromide 

Downstream Products

• 110270-52-5 (S)-2-benzyl-3-acetyloxy-1-propanol 
• 2612-30-8 2-benzyl-1,3-propanediol 
• 81110-73-8 N-(S-2-acetylthiomethyl-1-oxo-3-phenylpropyl)-glycine benzyl ester 
• 124815-67-4 (S)-2-acetylthiomethyl-3-phenylpropanoic acid 
• 195056-66-7 (R)-2-(acetoxymethyl)-3-phenylpropanoic acid 
• 123802-80-2 (R)-2-hydroxymethyl-3-phenylpropionic acid 
• 341925-86-8 benzyl (2S)-2-benzyl-3-[(t-butyloxycarbonyl)amino]propanoate 
• 341926-07-6 (2S)-2-benzyl-3-[(t-butyloxycarbonyl)amino]propyl acetate 
• 341926-08-7 (2S)-2-benzyl-3-[(t-butyloxycarbonyl)amino]propanol 
• 26250-90-8 (S)-2-[(tert-butoxycarbonylamino)methyl]-3-phenylpropanoic acid 
• 913546-09-5 (S)-2-benzyl-3-((tert-butyldimethylsilyl)oxy)propanal 
• 205380-73-0 (S)-2-benzyl-3-((tert-butyldimethylsilyl)oxy)-propyl acetate 
• 205380-74-1 (S)-2-benzyl-3-hydroxypropoxy tert-butyl dimethyl silane 
• 182365-57-7 2-Benzyl-3-<(tert-butyldimethylsilyl)oxy>-1-propanol 

Relevant academic research and scientific papers

An efficient enantioselective preparation of 2-substituted-3-hydroxypropionic acids via chemo-enzymatic reaction

The key intermediates, 2-substituted-3-hydroxypropionic acids 1, of the potent renin inhibitors were synthesized enantioselectively starting from 2-substituted-1,3-propanediols via chemo-enzymatic reaction.

New asymmetric synthesis of dexecadotril and ecadotril starting from a single precursor

We describe herein a method providing access to both enantiomers of 3-acetylthio-2-benzylpropionic acid via enzymatic desymmetrization of 2-benzyl-1,3-propanediol. These compounds are respectively the starting materials for the synthesis of ecadotril, and dexecadotril, which are powerful inhibitors of NEP (EC 3.4.24.11) and have been developed as therapeutic agents.

Lipase-based HPLC stationary phase: Enantioselective synthesis of 2- substituted 1,3-propanediol monoacetates

Pseudomonas cepacia lipase (PCL) has been immobilized by coating the enzyme on an epoxysilica HPLC column. The biocatalyst has been successfully used for the preparation of both the enantiomers of 3-acetoxy-2-benzyl- propan-1-ol and of 3-acetoxy-2-methylpropan-1-ol. The immobilized enzyme is active after months of use either in aqueous or in organic media. (C) 1999 Elsevier Science Ltd.

Optically active N- and C-terminal building blocks for the synthesis of peptidyl olefin peptidomimetics

Peptidyl olefin peptidomimetics serve as biologically active compounds or as intermediates for other peptidyl isosteres. The N-terminal side of the C=C bond could be easily prepared in an optically pure form from α-amino acids. Synthesis of C-terminal building blocks in an optically pure form is more challenging. We developed a chemoenzymatic stereoselective approach to such optically active C-terminal building blocks to be assembled into peptidyl olefins by a variety of reactions. They include an electrophilic aldehyde and nucleophilic sulfone, phosphonium salt, phosphonate, and diselenide. Key enzymatic hydrolysis of prochiral diesters to the corresponding hydroxy esters introduces optical activity. The sequence of the subsequent chemical reactions, either protection- hydrolysis-functionalization or functionalization-hydrolysis- protection, determines the absolute stereochemistry of the final building blocks.

Optically active γ-hydroxy sulfone Julia reagents for the synthesis of peptidyl olefin peptidomimetics

Peptidyl olefin peptidomimetics serve as biologically active compounds or as intermediates for other peptidyl isosteres. We developed a chemoenzymatic stereoselective approach to optically active γ-hydroxy sulfones to be assembled into peptidyl olefins by the Julia reaction. Key enzymatic hydrolysis of prochiral diesters to the corresponding hydroxy esters introduces optical activity. The sequence of the subsequent chemical reactions, either protection-hydrolysis-functionalization or functionalization-hydrolysis- protection, determines the absolute stereochemistry of the final sulfone building block. Wiley-VCH Verlag GmbH & Co. KGaA, 2008.

Chemoenzymatic synthesis of enantiomerically enriched α-chiral 3-oxy-propionaldehydes by lipase-catalyzed kinetic resolution and desymmetrization

Enantiomerically enriched phenylalanine- and leucine aldehyde analogues have been prepared by lipase catalyzed desymmetrization or kinetic resolution of 1,3-propanediol derivatives as key steps. Observations of unusual enantioselectivity were made, and mo

Asymmetric synthesis of homoisoflavanone using lipase-catalyzed reaction

The (R)- and (S)-enantiomers of 3-benzyl-4-chromanone (homoisoflavanone) were synthesized starting with the optically active 2-benzyl-1,3-propanediol monoacetates, which were obtained via the lipase-catalyzed enantioselective reaction.

Sulfonic acid ester derivatives, method for production thereof and use thereof

Novel and useful optical active 2-aralkyl-3-sulfonyloxy-1-propanol and 2-aralkyl-3-sulfonyloxypropionic acid are provided by using an optical active 2-aralkyl-3-acyloxy-1-propanol as a starting material. Furthermore, an optical active 2-aralkyl-3-thiopropionic acid, which is an important intermediate of enkephalinase inhibitor, is provided. According to the present invention, industrially useful optical active sulfonic acid ester derivatives can be provided.

Expanding the utility of proteases in synthesis: Broadening the substrate acceptance in non-coded amide bond formation using chemically modified mutants of subtilisin

The strategy of combined site directed mutagenesis and chemical modification creates chemically modified mutants (CMMs) with greatly broadened substrate specificities. We have previously reported that the CMMs of subtilisin Bacillus lentus (SBL) are efficient catalysts for the coupling of both L- and D-amino acids. We now report that these powerful catalysts also allow amide bond formation between a variety of non-coded carboxylic acids, including β-alanine and β-amino homologues of phenylalanine, with both L- and D-amino acid nucleophiles. As a guide to enzyme efficiency, a hydrolysis assay indicating pH change has been employed. CMMs selected by this screen furnished higher yields of coupling products compared to the wild-type enzyme (WT). Furthermore, both WT and CMM enzymes allow highly stereoselective aminolysis of a meso diester with an amino acid amine. These results highlight the utility of CMMs in the efficient formation of non-coded amides as potential peptide isosteres.

PROCESS FOR THE ASYMMETRIC SYNTHESIS OF S-ACYL DERIVATIVES OF 2-MERCAPTOMETHYL -3- PHENYL PROPANOIC ACID, APPLICATION TO THE SYNTHESIS OF N-(MERCAPTOACYL) AMINO ACID DERIVATIVES

Process for the asymmetric synthesis of S-acyl derivatives of 2-mercaptomethyl-3-phenylpropanoic acid of formula (I): characterized in that it comprises the steps consisting in:a) preparing the diol (VI) by reduction of a malonic ester (V) in the presence of a hydride; b) preparing the monoacetates (VII R) or (VII S) respectively; c) subjecting these monoacetates to an oxidation in order to form the acids (IX S) or (IX R);d) saponifying the compounds (IX S) or (IX R) in order to form the hydroxy acids (X S) or (X R);e) thioacylating the hydroxy acids (X S) or (X R) with a mercapto acid R. sub.1 SH (XI), according to a Mitsunobu-type reaction, in order to lead to the desired acids (I R) (I S) respectively and application to the synthesis of N-(mercaptoacyl)amino acid derivatives (II). STR1