17885-24-4Relevant articles and documents
S-Alk(en)ylmercaptocysteine: Chemical synthesis, biological activities, and redox-related mechanism
Zhang, Guodong,Parkin, Kirk L.
, p. 1896 - 1903 (2013)
S-Alk(en)ylmercaptocysteine (CySSR, R = methyl, ethyl, propyl, 1-propenyl, and allyl), which are the putative metabolites of Allium thiosulfinates, were chemically synthesized. CySSR, but not the corresponding monosulfide species S-alk(en)yl cysteine (CyS
A tissue homogenate method to prepare gram-scale allium thiosulfinates and their disulfide conjugates with cysteine and glutathione
Zhang, Guodong,Parkin, Kirk L.
, p. 3030 - 3038 (2013/08/25)
The health benefits of Allium vegetables are widely attributed to the enzyme-derived organosulfur compounds called thiosulfinates (TS). However, the lack of a suitable method to prepare TS in good yields has hampered the evaluation of their biological activities. This paper describe a simple enzymatic method using Allium tissue homogenates as a reaction system to prepare gram-scale TS, including those enriched in 1-propenyl groups, which are particularly difficult to obtain. This method is simple, easy to scale up, and requires no column purification step, making it suitable for practical large-scale production of Allium TS. The prepared TS were further utilized to prepare the disulfide conjugates with cysteine and glutathione (CySSR and GSSR, R = methyl, ethyl, propyl, 1-propenyl, and allyl), which are the presumptive metabolites of TS. Among all of the Allium CySSR and GSSR conjugates, the newly prepared glutathione conjugate with 1-propenyl TS, GSSPe, showed the most potent effect to induce quinone reductase (QR, a representative phase II enzyme) in murine hepatoma cells (Hepa 1c1c7) and inhibit nitric oxide (NO) production in lipopolysaccharide (LPS)-stimulated macrophage cells (RAW 264.7).
Selectively S-Protected Cysteine Peptides. IV. Synthesis of Cysteine Peptides Using the S-Ethylthio Protecting Group. II
Kunzek, Herbert,Rose, Karl-Berthold,Graetz, Solveyg,Nesener, Eckehard
, p. 186 - 198 (2007/10/02)
Studying the problems of the selective sulphur protection in cysteine peptides, a model octapeptide from the sheep insulin A-chain was prepared by conventional synthesis using the S-ethylthio and the S-diphenylmethyl group.As consequence of the small acid