77178-77-9

Basic information

• Product Name: Nα-Cbz-L-Methioninamide
• Synonyms: Nα-Cbz-L-Methioninamide
• CAS NO: 77178-77-9
• Molecular Formula: C₁₃H₁₈N₂O₃S
• Molecular Weight: 282.35862
• Mol File: 77178-77-9.mol

Chemical Properties

• Boiling Point: 523.6±50.0 °C(Predicted)
• Appearance: /
• Density: 1 +-.0.06 g/cm3(Predicted)
• PKA: 10.94±0.46(Predicted)
• CAS DataBase Reference: Nα-Cbz-L-Methioninamide(CAS DataBase Reference)
• NIST Chemistry Reference: Nα-Cbz-L-Methioninamide(77178-77-9)
• EPA Substance Registry System: Nα-Cbz-L-Methioninamide(77178-77-9)

Safety Data

• Hazardous Substances Data: 77178-77-9(Hazardous Substances Data)

Upstream product

• 56762-93-7 methyl (S)-2-(benzyloxycarbonylamino)-4-methylmercaptobutanoate 
• 1152-62-1 Cbz-Met-OH 

Downstream Products

• 33876-11-8 ((S)-1-Cyano-3-methylsulfanyl-propyl)-carbamic acid benzyl ester 

Relevant articles and documents

Amidation of carboxylic acids via the mixed carbonic carboxylic anhydrides and its application to synthesis of antidepressant (1S,2R)-tranylcypromine

Primary amidations of carboxylic acids 1 or 3 with NH4Cl in the presence of ClCO2Et and Et3N were developed to afford the corresponding primary amides in 22% to quantitative yields. Additionally, we have applied the amidation to the preparation of various amides containing hydroxamic acids and achieved the synthesis of (1S,2R)-tranylcypromine as an antidepressant medicine via Lossen rearrangement.

Convenient preparation of primary amides via activation of carboxylic acids with ethyl chloroformate and triethylamine under mild conditions

Primary amides were easily prepared in 22-99% yields from the corresponding carboxylic acids 1 or 5 with NH4Cl via activation with ClCO 2Et and Et3N. The enantiomers of the corresponding primary amides of Cbz-, Boc-, or Fmoc-α-amino acids can be separated by using a chiral column.

Enzymatic C-terminal amidation of amino acids and peptides

Herein, we describe two versatile and high yielding enzymatic approaches for the conversion of semi-protected amino acid and peptidyl C-terminal α-carboxylic acids into their corresponding amides. In the first approach, the lipase Candida antarctica lipase-B (Cal-B), and in the second approach, the protease Subtilisin A, are used, respectively. We found that by using the ammonium salt of the α-carboxylic acid instead of separate ammonia sources, the enzymatic amidation reactions proceeded much faster without side reactions and gave near to quantitative yields of products.