17193-30-5

Upstream product

• 77128-73-5 (2S)-N-fluorenylmethyloxycarbonyl-2-amino-N-methyl-3-phenylpropanoic acid 
• 2899-07-2 (S)-N-benzyloxycarbonyl-N-methyl-phenyl alanine 
• 2566-30-5 N-Methyl-L-phenylalanine 
• 2812-24-0 (S)-ethyl-2-(methylamino)-3-phenylpropanoate 

Downstream Products

• 2566-30-5 N-Methyl-L-phenylalanine 
• 56564-52-4 N-methyl-D-phenylalanine 
• 157974-05-5 Boc-Gly-N-MePhe-NH₂ 
• 157974-11-3 {2-[((S)-1-Carbamoyl-2-phenyl-ethyl)-methyl-carbamoyl]-ethyl}-methyl-carbamic acid tert-butyl ester 
• 157974-15-7 {3-[((S)-1-Carbamoyl-2-phenyl-ethyl)-methyl-carbamoyl]-propyl}-methyl-carbamic acid benzyl ester 
• 134675-58-4 Boc-Trp-3PP-Asp(OBn)-(N-Me)Phe-NH₂ 
• 134676-16-7 (S)-N-((S)-1-Carbamoyl-2-phenyl-ethyl)-N-methyl-3-[((2S,3S)-3-propyl-pyrrolidine-2-carbonyl)-amino]-succinamic acid benzyl ester; hydrochloride 
• 131450-72-1 H-Asp(OBn)-N(Me)Phe-NH₂ hydrochloride salt 
• 134676-15-6 Boc-3PP-Asp(OBn)-(N-Me)Phe-NH₂ 

Relevant academic research and scientific papers

Chemical models of peptide formation in translation

Ribosomal incorporations of N-alkyl amino acids including proline are slower than incorporations of non-N-alkyl L-amino acids. The chemical reactivity hypothesis proposes that these results and the exclusion of nonproline N-alkyl amino acids from the gene

Synthesis of optically active α-methylamino acids and amides through biocatalytic kinetic resolution of amides

Catalyzed by Rhodococcus sp. AJ270, a nitrile hydratase and amidase containing microbial whole-cell catalyst, under very mild conditions, a number of racemic α-methylamino amides were resolved into the corresponding optically active (S)-(+)-α-methylamino acids and (R)-(-)-α- methylamino amides. The steric requirement of the amidase against α-amino phenylacetamides bearing methyl group(s) at α-amino nitrogen and/or α-carbon was also studied. Coupled with the chemical hydrolysis of amide, the biotransformation process provided a direct synthesis of α-methylamino acids in both enantiomeric forms from readily available racemic amides.

Development of Potent and Selective CCK-A Receptor Agonists from Boc-CCK-4: Tetrapeptides Containing Lys(Nε)-Amide Residues

A series of Boc-CCK-4 derivatives represented by the general structure Boc-Trp-Lys(Nε-COR)-Asp-Phe-NH2, where R is an aromatic, heterocyclic, or aliphatic group, are potent and selective CCK-A receptor agonists.These amide-bearing compounds complement the previously described urea-based tetrapeptides (Shiosaki et al.J.Med.Chem. 1991,34,2837-2842); structure-activity studies revealed parallel as well as divergent trends between these two series.A significant correlation was observed between pancreatic binding affinity and the resonance constant R of the phenyl substituent in one particular series of derivatives.Sulfation of phenolic amides appended onto the ε-amino group of the lysine did not affect affinity for the CCK-A receptor in contrast to the 500-fold increase in binding potency observed upon sulfation of CCK-8, suggesting that the lysine appendage and the sulfated tyrosine in CCK-8, both key structural elements that impart high affinity for the CCK-A receptor, are interacting differently with the receptor.The amide-bearing tetrapeptides are full agonists relative to CCK-8 in stimulating pancreatic amylase release while being partial agonists in eliciting phosphoinositide (PI) hydrolysis.Both effects were blocked by selective CCK-A receptor antagonists

Diazepinoquinolines with L-Amino Acid Moiety - Preparation and Reactions

Quaternary salts of the amides of N-(3-quinolinecarbonyl)-N-alkyl-amino acids (6) cyclise under the influence of base to the title compounds (7).This intramolecular addition is a reaction with high diastereoselectivity, dependent on the amino acid part. 7