14441-07-7

Upstream product

• 922705-36-0 (4R)-N-benzyloxycarbonyl-4-phenyl-1,3-oxazinan-6-one 
• 126575-05-1 DL-3-(N-formylamino)-3-phenylpropionic acid 
• 3082-67-5 L-3-(N-formylamino)-3-phenylpropionic acid 
• 228861-79-8 N^α-Z-phenylglycinyldiazomethane 
• 501-53-1 benzyl chloroformate 
• 83649-48-3 (R)-3-amino-3-phenylpropionic acid hydrochloride 
• 5491-18-9 (S)-N-(benzyloxycarbonyl)phenylglycine 

Downstream Products

• 875574-87-1 (S)-methyl 2-((R)-3-(benzyloxycarbonylamino)-3-phenylpropanamido)-5-(1,3-dioxolan-2-yl)pentanoate 

Relevant academic research and scientific papers

A convenient method for the synthesis of β-amino acids via the Arndt-Eistert approach using p-toluenesulphonyl chloride as a carboxylic group activating agent

A simple method for the synthesis of Z-/Boc-/Fmoc-protected β-amino acids by the Arndt-Eistert approach employing p-toluenesulphonyl chloride for the activation of the carboxyl group of Nα-protected amino acid is described. The method is rapid and gave good yields with opitical purity.

Diastereoselective synthesis of α-methyl and α-hydroxy-β- amino acids via 4-substituted-1,3-oxazinan-6-ones

(Chemical Equation Presented) 1,3-Oxazinan-6-ones have been utilized in a series of enolate reactions to produce 5-hydroxy and 5-alkyl-4-substituted-1,3- oxazinan-6-ones with excellent trans diastereoselectivity. Highlighting the versatility of the oxazin

Wolff rearrangement of Nα-Boc-/Z-protected aminodiazoketones to the corresponding β-amino acids under microwave irradiation

The Wolff rearrangement of Nα-Boc-/Z-protected aminodiazoketones in the presence of silver benzoate under microwave irradiation is described. The reaction is found to be rapid, efficient and complete. It results in the isolation of Boc-/Z- prot

Synthesis of Fmoc-/Boc-/Z-β-amino acids via Arndt-Eistert homologation of Fmoc-/Boc-/Z-α-amino acids employing BOP and PyBOP

A simple and efficient protocol for Arndt-Eistert chain homologation of Fmoc-/Boc-/Z-α-amino acids using BOP or PyBOP as a coupling agent to the corresponding β-amino acids, synthesizing the key intermediate α-diazoketones as crystalline solids in good yield is described.

THIADIAZOLE AMIDE MMP INHIBITORS

The present invention provides novel thiadiazole amide derivatives represented by formula I The compounds of the present invention inhibit various enzymes from the matrix metalloproteinase family, predominantly stromelysins, and hence are useful f

Homologation of α-amino acids to β-amino acids using Boc2O

The use of Boc2O as a coupling agent in the homologation of N-urethane protected-α-amino acid to its β-homomers by the Arndt-Eistert method is described. The homologation gives good yields without racemization. The use of Boc2O as a

THIADIAZOLE AMIDE MMP INHIBITORS

The present invention provides novel thiadiazole amide derivatives represented by formula I STR1 The compounds of the present invention inhibit various enzymes from the matrix metalloproteinase family, predominantly stromelysins, and hence are useful for

Analogues of 2'(3')-O-L-phenylalanyladenosine as substrates and inhibitors of ribosomal peptidyltransferase

The chemical syntheses of 2'(3')-O-(L-3-amino-3-phenylpropionyl)adenosine (2e), the corresponding D stereoisomer 2f, 2'(3')-O-(DL-phenylglycyl)adenosine (2g), 2'(3')-O-(N-benzylglycyl)adenosine (2h), and 9-(2-O-L-phenylalanyl-β-D-xylofuranosyl)adenine (3b) are described. Compounds 2e-h were obtained by acylation of 5'-O(4-methoxytrityl)adenosine with the appropriate N-benzyloxycarbonyl or N-tert-butoxycarbonyl amino acids with dicyclohexylcarbodiimide in pyridine. The corresponding reaction of N-(benzyloxycarbonyl)-D-phenylglycine led to an almost complete racemization of the aminoacyl residue (compounds 2c and 2g). Subsequent chromatographic separation and deprotection of intermediates 2a-d afforded the desired target derivatives 2e-h. Product 3b was obtained by a similar acylation of 9-(3,5-O-isopropylidene-β-D-xylofuranosyl)adenine with N-(benzyloxycarbonyl)-L-phenylalanine, followed by deblocking. The NMR spectra of 2' and 3' isomers of stereoisomers 2a and 2b are discussed. Compounds 2g and 3b are both substrates and inhibitors of Escherichia coli ribosomal peptidyltransferase, although the activity of 3b is low. Derivatives 2e,f,h do not accept AcPhe from N-AcPhe-tRNA in a peptidyltransferase-catalyzed reaction, but they inhibit the puromycin reaction in the same system. The order of inhibitory activity is 2e>2f>2h. The implications of these findings for the mechanism of peptidyltransferase and comparison of the latter with the action of chymotrypsin are discussed.