65278-03-7Relevant academic research and scientific papers
Tuning of protease resistance in oligopeptides through: N -alkylation
Kaminker, Revital,Anastasaki, Athina,Gutekunst, Will R.,Luo, Yingdong,Lee, Sang-Ho,Hawker, Craig J.
supporting information, p. 9631 - 9634 (2018/09/10)
N-Methylation of amino acids is an effective way to create protease resistance in both natural and synthetic peptides. However, alkyl substituents other than N-methyl have not been extensively studied. Here, we prepare and examine a series of N-substituted peptides in which the size and length of the alkyl group is modulated. These design insights provide a unique and modular handle for tuning proteolysis in oligopeptides.
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.
Synthesis of α-N-ethylamino acids and their derivatives
Schedel, Hartmut,Burger, Klaus
, p. 1011 - 1018 (2007/10/03)
A new synthesis of α-N-ethylamino acids starting from α-amino acids using hexafluoroacetone as protecting and activating agent is described. The hexafluoroacetone-protected N-ethylamino acid derivatives obtained are activated lactons. Therefore, they can be directly transformed without the need of an additional activation step with various nucleophiles into the corresponding carboxylic acid derivatives.
