96193-68-9Relevant academic research and scientific papers
Control of lysyl oxidase activity through site-specific deuteration of lysine
Pestov, Nikolay B.,Okkelman, Irina A.,Shmanai, Vadim V.,Hurski, Alaksiej L.,Giaccia, Amato J.,Shchepinov, Mikhail S.
experimental part, p. 255 - 258 (2011/02/25)
Lysyl oxidase (LOX) is implicated in several extracellular matrix related disorders, including fibrosis and cancer. Methods of inhibition of LOX in vivo include antibodies, copper sequestration and toxic small molecules such as β-aminopropionitrile. Here,
THERAPIES FOR CANCER USING ISOTOPICALLY SUBSTITUTED LYSINE
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Page/Page column 7, (2009/10/22)
Methods of treatment and substances for treatment of cancer may use or cause the creation of isotopically modified lysine at levels that do not occur naturally.
N-trifluoroacyl lysine derivatives in the synthesis of L-lysyl-L-glutamic acid
Cherevin,Gulevich,Popova,Zubreichuk,Knizhnikov
, p. 1427 - 1431 (2008/09/16)
Conditions were developed for simultaneous preparation of N a-trifluoroacetyl-L-lysine and N α,N a-bis(trifluoroacetyl)-L-lysine at overall conversion of initial lysine monohydrochloride up to 82%. By reaction of dimethyl L-glutamate with N α,N a-bis(trifluoroacetyl)-L-lysyl chloride in the presence of triethylamine or with N α- carboxyanhydride of N a-trifluoroacetyl-L-lysine with subsequent removing protecting groups in the formed dipeptides by treating with water-ethanol solution of sodium hydroxide we obtained L-lysyl-L-glutamic acid. Physicochemical characteristics of samples obtained coincided with characteristics of L-lysyl-L-glutamic acid described in the literature thus suggesting that no racemization occurred either at the stage of peptide bond formation or at deprotection.
