770742-93-3

Usage

Uses

S-Allyl-L-cysteine exhibits neuroprotective properties.

Upstream product

• 52467-58-0 S-allyl-N-formyl-DL-cysteine 
• 921-01-7 D-cysteine 
• 107-05-1 3-chloroprop-1-ene 
• 49621-03-6 S-propenyl-L-cysteine 
• 32443-99-5 D-cysteine hydrochloride 
• 106-95-6 allyl bromide 

Downstream Products

• 1195577-61-7 (S)-allyl-L-cysteine sulfoxide 
• 556-27-4 3-((S)-prop-2-ene-1-sulfinyl)-D-alanine 

Relevant academic research and scientific papers

IMPROVEMENTS IN OR RELATING TO ALLIUM EXTRACTS

The present invention relates to improvements in or relating to Allium extracts. In particular, it relates to improvements in or relating to extending the therapeutic half- life or duration of Allium extracts. The invention also relates to the synthesis of certain thiosulfinate compounds, especially to the synthesis of methyl allyl thiosulfinate and allyl methyl thiosulfinate, in particular from either methiin or alliin alone or a mixture of both. The invention further relates to the synthesis of methyl allyl thiosulfinate, allyl methyl thiosulfinate, allicin, and methyl methyl thiosulfinate in a mixture with varying molar or mass ratios depending on the reaction conditions, in particular from either methiin or alliin alone or a mixture of both. A high yielding, optimized synthesis of allicin starts from alliin, whereas methyl methyl thiosulfinate is advantageously obtained from methiin. Also provided is a kit comprising methiin in a first container and/or alliin in a second container and an allinase source, in particular garlic powder in a third container. Finally, the invention provides a method of preparing a mixture of methyl allyl thiosulfinate, allyl methyl thiosulfinate, allyl allyl thiosulfinate (allicin) and methyl methyl thiosulfinate from methiin and pieces of an Allium species.

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.