197902-88-8

Upstream product

• 136159-65-4 (R)-4-benzyl-3-(3-phenyl-propionyl)-oxazolidin-2-one 
• 1104950-94-8 C₂₇H₂₈N₂O₄ 
• 748127-65-3 methyl 2-[(benzyloxyamino)methyl]-3-phenylpropionate 
• 709673-94-9 (R)-2-benzyl-3-hydroxypropanoic acid methyl ester 
• 220805-30-1 (S)-4-Benzyl-3-((R)-2-benzyloxymethyl-3-phenyl-propionyl)-oxazolidin-2-one 
• 123803-51-0 2R-benzyl-3-benzyloxypropanoic acid 
• 218285-61-1 (R)-N-Benzyloxy-2-hydroxymethyl-3-phenyl-propionamide 
• 2687-43-6 O-benzylhydoxylamine hydrochloride 
• 123802-80-2 (R)-2-hydroxymethyl-3-phenylpropionic acid 
• 218285-65-5 (3R)-N-benzyloxy-3-benzyl-2-azetidinone 

Downstream Products

• 748127-65-3 methyl 2-[(benzyloxyamino)methyl]-3-phenylpropionate 
• 269396-38-5 (4S,7S,12bR)-7-[(R)-2-(Benzyloxyamino-methyl)-3-phenyl-propionylamino]-6-oxo-1,2,3,4,6,7,8,12b-octahydro-benzo[c]pyrido[1,2-a]azepine-4-carboxylic acid methyl ester 
• 440679-71-0 (R)-2-[(Formyl-hydroxy-amino)-methyl]-N-((S)-1-hydroxy-2-oxo-azepan-3-yl)-3-phenyl-propionamide 
• 440679-76-5 (R)-2-[(Benzyloxy-formyl-amino)-methyl]-N-((S)-1-hydroxy-2-oxo-azepan-3-yl)-3-phenyl-propionamide 
• 944030-55-1 C₁₈H₁₉NO₄ 
• 1354899-35-6 (S)-2-[(R)-2-benzyl-3-(formyl-hydroxy-amino)-propionylamino]-3,3,N-trimethyl-butyramide 
• 1354899-38-9 C₁₈H₂₇N₃O₄ 
• 1354899-39-0 (R)-2-benzyl-3-(formyl-hydroxy-amino)-N-[(S)-1-methylcarbamoyl-2-phenyl-ethyl]-propionamide 
• 440679-75-4 (R)-2-(Benzyloxyamino-methyl)-N-((S)-1-hydroxy-2-oxo-azepan-3-yl)-3-phenyl-propionamide 
• 183182-07-2 (R)-α-benzyl-β-aminopropanoic acid 

Relevant academic research and scientific papers

Reverse Hydroxamate Inhibitors of Bone Morphogenetic Protein 1

Bone Morphogenetic Protein 1 (BMP1) inhibition is a potential method for treating fibrosis because BMP1, a member of the zinc metalloprotease family, is required to convert pro-collagen to collagen. A novel class of reverse hydroxamate BMP1 inhibitors was

Inhibition of invasion and capillary-like tube formation by retrohydroxamate-based MMP inhibitors

Matrix metalloproteinases (MMPs), a family of zinc-containing endopeptidases, participate in many normal processes such as embryonic development and wound repair, and in many pathological situations such as cancer, atherosclerosis, and arthritis. Peptidomimetic MMP inhibitors were designed and synthesized with Nformylhydroxylamine (retrohydroxamate) as a zinc-binding group and various side chains on the α, P1′, and P2′ positions. Using in vitro MMP assays with purified MMPs (MMP-1, MMP-2, MMP-3, MMP-9, and MMP-14) and fluorogenic peptide substrates, it was found that compounds 2d and 2g selectively inhibit gelatinases (MMP-2 and MMP-9) and interstitial collagenase (MMP-1). They also inhibited the chemo-invasion of fibrosarcoma HT-1080 cells and tube formation of human umbilical vascular endothelial cells in a dosedependent manner. Our results suggest that retrohydroxamate-based MMP inhibitors, especially compounds 2d and 2g, have the potential to be used as therapeutic drugs for cancer and other MMP-related diseases.

A general approach to the synthesis of β2-amino acid derivatives via highly efficient catalytic asymmetric hydrogenation of α-aminomethylacrylates

A new strategy was developed for the synthesis of a valuable class of α-aminomethylacrylates via the Baylis-Hillman reaction of different aldehydes with methyl acrylate followed by acetylation of the resulting allylic alcohols and SN2′-type amination of the allylic acetates. Asymmetric hydrogenation of these diverse olefinic precursors using rhodium(Et-Duphos) catalysts provided the corresponding β2-amino acid derivatives with excellent enantioselectivities and exceedingly high reactivities (up to >99.5% ee and S/C=10,000). The first hydrogenation of (Z)-configurated substrates was studied for the synthesis of β2-amino acid derivatives. The high influence of the substrate geometry and steric hindrance on the reactivity and enantioselectivity was also disclosed for this reaction. This protocol provides a highly practical, facile and scalable method for the preparation of optically pure β2- amino acids and their derivatives under mild reaction conditions.

Peptide deformylase inhibitors of Mycobacterium tuberculosis: Synthesis, structural investigations, and biological results

Bacterial peptide deformylase (PDF) belongs to a subfamily of metalloproteases catalyzing the removal of the N-terminal formyl group from newly synthesized proteins. We report the synthesis and biological activity of highly potent inhibitors of Mycobacterium tuberculosis (Mtb) PDF enzyme as well as the first X-ray crystal structure of Mtb PDF. Structure-activity relationship and crystallographic data clarified the structural requirements for high enzyme potency and cell based potency. Activities against single and multi-drug-resistant Mtb strains are also reported.

Synthesis and Biological Activity of Hydroxamic Acid-Derived Vasopeptidase Inhibitor Analogues

(Equation Presented) Syntheses of novel hydroxamic acid-derived azepinones containing pendant mercaptoacyl groups or formyl hydroxamates are described. These new analogues of therapeutically important ACE and NEP inhibitors include unprecedented changes a

First hydroxamate inhibitors for carboxypeptidase A. N-acyl-N-hydroxy- β-phenylalanine S

A series of N-acyl-N-hydroxy-β-Phe were designed, synthesized, and shown to have potent inhibitory activity for carboxypeptidase A (CPA). They are the first examples of CPA inhibitors having a hydroxamate functionality.

A practical method for the conversion of β-hydroxy carboxylic acids into the corresponding β-amino acids

Optically active α- or β-substituted βamino acids were synthesized from the corresponding β-hydroxy acids in 4 steps in excellent yield. Stereochemistry was retained at the α-position and reversed at the β-position during the conversion.