21691-41-8Relevant articles and documents
Trimethyl-substituted carbamate as a versatile self-immolative linker for fluorescence detection of enzyme reactions
Inoue, Kazuya,Nakamura, Noriaki,Ojida, Akio,Uchinomiya, Shohei
supporting information, (2020/05/25)
Self-immolative linker is a useful building block of molecular probes, with broad applications in the fields of enzyme activity analysis, stimuli-responsive material science, and drug delivery. This manuscript presents N-methyl dimethyl methyl (i.e., trimethyl) carbamate as a new class of self-immolative linker for the fluorescence detection of enzyme reactions. The trimethyl carbamate was shown to spontaneously undergo intramolecular cyclization upon formation of a carboxylate group, to liberate a fluorophore with the second time rapid reaction kinetics. Interestingly, the auto-cleavage reaction of trimethyl carbamate was also induced by the formation of hydroxyl and amino groups. Fluorescent probes with a trimethyl carbamate could be applicable for fluorescence monitoring of the enzyme reactions catalyzed by esterase, ketoreductase, and aminotransferase, and for fluorescence imaging of intracellular esterase activity in living cells, hence demonstrating the utility of this new class of self-immolative linker.
Synthesis of N-alkyl-N-methyl amino acids. Scope and limitations of base-induced N-alkylation of Cbz-amino acids
Stodulski, Maciej,Mlynarski, Jacek
, p. 970 - 975 (2008/09/21)
The reaction of N-benzyloxycarbonyl derivatives of aliphatic amino acids with NaH/alkyl iodides gave the corresponding N-Cbz-N-alkyl derivatives in good to high yields. The scope and limitations of this simple N-alkylation reaction were investigated as a convenient and flexible attempt to prepare unsymmetrically N,N-diprotected α-amino acids. The procedure is based on the N-alkylation of N-carbamoyl amino acids, a one-pot deprotection/protection sequence without extensive purification of the products. Protection of the carboxyl function is not required while the starting materials are inexpensive and commercially available.
Effective methods for the synthesis of N-methyl β-amino acids from all twenty common α-amino acids using 1,3-oxazolidin-5-ones and 1,3-oxazinan-6-ones
Hughes, Andrew B.,Sleebs, Brad E.
, p. 2611 - 2637 (2007/10/03)
N-Methyl β-amino acids are generally required for application in the synthesis of potentially bioactive modified peptides and other oligomers. Previous work highlighted the reductive cleavage of 1,3-oxazolidin-5-ones to synthesise N-methyl α-amino acids. Starting from α-amino acids, two approaches were used to prepare the corresponding N-methyl β-amino acids. First, α-amino acids were converted to N-methyl α-amino acids by the so-called '1,3-oxazolidin-5-one strategy', and these were then homologated by the Arndt-Eistert procedure to afford N-protected N-methyl β-amino acids derived from the 20 common α-amino acids. These compounds were prepared in yields of 23-57% (relative to N-methyl α-amino acid). In a second approach, twelve N-protected α-amino acids could be directly homologated by the Arndt-Eistert procedure, and the resulting β-amino acids were converted to the 1,3-oxazinan-6-ones in 30-45% yield. Finally, reductive cleavage afforded the desired N-methyl β-amino acids in 41-63% yield. One sterically congested β-amino acid, 3-methyl-3-aminobutanoic acid, did give a high yield (95%) of the 1,3-oxazinan-6-one (65), and subsequent reductive cleavage gave the corresponding AIBN-derived N-methyl β-amino acid 61 in 71% yield (Scheme 2). Thus, our protocols allow the ready preparation of all N-methyl β-amino acids derived from the 20 proteinogenic α-amino acids.
A simple and rapid protocol for N-methyl-α-amino acids
Reddy, G. Vidyasagar,Iyengar
, p. 299 - 300 (2007/10/03)
A two step strategy for optically pure N-Protected-N-methyl-α-amino acids starting from N-protected-α-amino acids via reductive cleavage of oxazolidinones using NaCNBH3/TMSCl is described.
Preparation of optically active ketones
-
, (2008/06/13)
An optically active alpha-amino acid derivative having the formula: STR1 wherein: X is OH, Cl, Br, I, or OCOR3 ; Y is a radical selected to stabilize the alpha carbon atom of the alpha-amino acid derivative sufficiently to prevent significant change in symmetry thereof during replacement of X with an alkyl, aryl, alkenyl, alkynyl, alkaryl, aralkyl, alkenaryl or alkynaryl radical, or such radical having one or more chemical constituents thereon; and R1 and R2 are different from one another and are each hydrogen or an alkyl, aryl, alkenyl, alkynyl, alkaryl, aralkyl, alkenaryl, or alkynaryl radical, or such radical having one or more non-protic chemical constituents thereon is conventionally synthesized from the corresponding alpha-amino acid. The STR2 portion of the above derivative is converted to a ketone functionality without racemization.
Aqueous Solutions Containing Amino Acids and Peptides. Part 22 - Free Energetic and Enthalpic Virial Coefficients at 25 deg C for Some Interactions of Isofunctional Amides
Blackburn, G. Michael,Lilley, Terence H.,Milburn, Peter J.
, p. 99 - 108 (2007/10/02)
The excess free energies of aqueous solutions containing N-acetyl-L-prolinamide, N-acetyl-N-methyl-L-alaninamide and binary mixtures of these have been determined at 25 deg C from isopiestic measurements.The corresponding excess enthalpies for the last tw
SUBSTITUTED PEPTIDE COMPOUNDS
-
, (2008/06/13)
Substituted peptide compounds of the formula STR1 are disclosed. These compounds are useful as hypotensive agents due to their angiotensin converting enzyme inhibition activity and depending upon the definition of X may also be useful as analgesics due to their enkephalinase inhibition activity.
