1190-48-3Relevant academic research and scientific papers
Molecular rotations of N(α)-acyl-L-lysines at various pH values
Soejima,Akagi,Izumiya
, p. 2618 - 2620 (1994)
Molecular rotations of N(α)-acyl-L-lysines were determined in water and in water containing various amounts of HCl or NaOH. The acyl groups were formyl, acetyl, propionyl, and butyryl. Each N(α)-acyl-L-lysine exhibited more negative rotation in HCl or NaOH solution than in water. The plot of molecular rotation against amount of HCl or NaOH resembled that of a D-α-amino acid even though N(α)-acyl-lysine was of L-form. The reason for this is discussed from the standpoint of steric factors. N(ε)-Acyl-L-lysines corresponding to the N(α)-acyl-L-lysines were synthesized as reference compounds. It was found that water-soluble N(ε)-acyl-L-lysines can be easily prepared by acylation of the Cu complex solution of L-lysine hydrochloride in the presence of triethylamine. The molecular rotation plots for N(ε)-acyl-L-lysines were typical of L-α-amino acids.
Degradation of 1-deoxy-d-erythro-hexo-2,3-diulose in the presence of lysine leads to formation of carboxylic acid amides
Smuda, Mareen,Voigt, Michael,Glomb, Marcus A.
experimental part, p. 6458 - 6464 (2011/08/09)
A novel species of amides formed from degradation of one of the most important key intermediates in Maillard hexose chemistry-1-deoxyhexo-2,3- diulose-was investigated. In 1-deoxyhexo-2,3-diulose/Nα-t-BOC- lysine reaction mixtures four amides, Nε-acetyl lysine, N ε-formyl lysine, Nε-lactoyl lysine and N ε-glycerinyl lysine, were identified and their structures verified by authentic reference standards. Amides and corresponding carboxylic acids (acetic acid, formic acid, lactic acid and glyceric acid) accumulated over time. Both Nε-lysine amides and carboxylic acids were thus determined as stable Maillard end products. Results of model incubations suggested the synthesis of amides to be mechanistically closely related to the formation of their corresponding carboxylic acids by β-dicarbonyl cleavage. Due to the different chemical properties of all the compounds monitored, various analytical strategies had to be carried out (LC-MS2, GC-MS, GC-FID, enzymatic determination).
Acylation of protein lysines by trichloroethylene oxide
Cai, Hongliang,Guengerich, F. Peter
, p. 327 - 335 (2007/10/03)
Stable lysine adducts were formed in proteins following reaction with trichloroethylene (TCE) oxide, the major reactive compound generated by the metabolism of TCE. The order of formation of these adducts is N6- formyllysine > N6-(dichloroacetyl)lysine >> N6-glyoxyllysine, with the ratio being influenced by the particular protein. Protein lysine adducts were also analyzed following the enzymatic oxidation of TCE with several different cytochrome P450 (P450) enzyme systems. The ratio of formyl/dichloroacetyl lysine adducts was influenced by the enzyme system that was used. Chloral and TCE oxide formation was more extensive with rat liver microsomes isolated from phenobarbital-treated rats than with rat microsomes in which P450 2E1 was induced by treatment with isoniazid or in human P450 2E1 systems. Glutathione (GSH) and GSH transferase had inhibitory effects on the reaction of TCE oxide with albumin, with formylation being attenuated much more than the formation of dichloroacetyllysine. GSH is likely to react with the reactive acyl chloride intermediates formed from TCE oxide hydrolysis, instead of direct reaction with TCE oxide, as judged by the lack of an effect of GSH on the rate of decomposition of TCE oxide. Studies with the model enzymes aldolase and glucose-6-phosphate dehydrogenase, both known to have sensitive lysine groups, indicate that TCE oxide has effects similar to known acylating agents that form the same adducts; concentrations of TCE oxide (or the model acylating agents) in the low-millimolar range were needed for inhibition. The characterization of TCE-derived protein adducts can be used as a basis for consideration of the exposure and risk of TCE to humans. Human P450 2E1 was less likely to oxidize TCE to form TCE oxide and protein lysine adducts than rat P450 2B1, and the difference is rationalized in terms of the influence of the protein on chloride migration in an enzyme reaction intermediate.
A new formylating reagent: N-(diethylcarbamoyl)-N-methoxyformamide
Akikusa,Mitsui,Sakamoto,Kikugawa
, p. 1058 - 1060 (2007/10/02)
A simple and efficient method for the direct chemoselective formylation of primary amines in the presence of alcohols or secondary amines using a new reagent, N-(diethylcarbamoyl)-N-methoxyformamide is described.
