204711-93-3

Upstream product

• 1119-60-4 hept-6-enoic acid 
• 101711-90-4 (S)-4-benzyl-2-oxazolidinone lithium salt 
• 52485-73-1 1,2-epoxy-7-octene 
• 21430-12-6 6-heptenoyl chloride 
• 90719-32-7 (S)-4-Benzyl-2-oxazolidinone 
• 3710-30-3 1,7-Octadiene 
• 17206-61-0 hept-6-enal 

Downstream Products

• 204711-94-4 (S)-3-((S)-2-Azido-hept-6-enoyl)-4-benzyl-oxazolidin-2-one 
• 219546-21-1 (S)-4-Benzyl-3-((S)-2-methyl-hept-6-enoyl)-oxazolidin-2-one 
• 596111-57-8 N-benzyloxy-α-(4-penten-1-yl)-β-lactam 
• 596111-53-4 2R-[(N-benzyloxy-N-formylamino)methyl]-6-heptenoic acid 
• 596111-58-9 2R-[(benzyloxyamino)methyl]-6-heptenoic acid 
• 596111-56-7 N-benzyloxy-2R-hydroxymethyl-6-heptenamide 
• 596111-59-0 N-(3-tert-butyl-2,5-dioxo-1,4-diaza-cyclopentadec-10-en-6-ylmethyl)-N-benzyloxyformamide 
• 596111-52-3 N^α-{[(2R-N-benzyloxy-N-formylamino)methyl]-6-heptenoyl}-N-(5-hexen-1-yl)-L-tert-leucinamide 
• 204711-95-5 [(S)-1-((S)-4-Benzyl-2-oxo-oxazolidine-3-carbonyl)-hex-5-enyl]-carbamic acid tert-butyl ester 
• 204711-97-7 (2S)-2-[(tert-butoxycarbonyl)amino]hept-6-enoic acid 
• 596111-55-6 4S-benzyl-3-(2R-hydroxymethyl-6-heptenoyl)-oxazolidin-2-one 

Relevant academic research and scientific papers

Potent inhibitors of the hepatitis C virus NS3 protease: Design and synthesis of macrocyclic substrate-based β-strand mimics

The virally encoded NS3 protease is essential to the life cycle of the hepatitis C virus (HCV), an important human pathogen causing chronic hepatitis, cirrhosis of the liver, and hepatocellular carcinoma. The design and synthesis of 15-membered ring β-strand mimics which are capable of inhibiting the interactions between the HCV NS3 protease enzyme and its polyprotein substrate will be described. The binding interactions between a macrocyclic ligand and the enzyme were explored by NMR and molecular dynamics, and a model of the ligand/enzyme complex was developed.

Structure-based design of a macrocyclic inhibitor for peptide deformylase

A macrocyclic, peptidomimetic inhibitor of peptide deformylase was designed by covalently cross-linking the P1′ and P3′ side chains. The macrocycle, which contains an N-formylhydroxylamine side chain as the metal-chelating group, was synthesized from a diene precursor via olefin metathesis using Grubbs's catalyst. The cyclic inhibitor showed potent inhibitory activity toward Escherichia coli deformylase (Ki = 0.67 nM) and antibacterial activity against both Gram-positive and Gram-negative bacteria (MIC = 0.7-12 μg/mL).

Synthesis of novel cyclic protease inhibitors using Grubbs olefin metathesis

The unusual amino acid bishomoallylglycine was synthesized and used to form cyclic P3-P1 tripeptide inhibitors via a Grubbs olefin metathesis method. These compounds show micro- to nanomolar inhibition of Rhizopus chinensis pepsin and represent a new class of simplified aspartic protease inhibitors lacking P' residues.