455-60-7

Upstream product

• 616-06-8 2-amino-hexanoic acid 
• 383-64-2 S-ethyl trifluoroacetate 
• 354-32-5 trifluoracetyl chloride 
• 383-63-1 ethyl trifluoroacetate, 
• 60-32-2 6-aminohexanoic acid 
• 24356-14-7 tert-Butyl 2R-Bromo-5-methylpentanoate 
• 29588-35-0 2-(2,2,2-Trifluoro-acetylamino)-hexanoic acid tert-butyl ester 

Relevant academic research and scientific papers

Nucleotide oligomer, nucleotide polymer, method for determining structure of functional substance and method for manufacturing functional substance

A modified nucleotide n-mer (where n is an integer of 2 or more) is used which comprises a nucleoside unit with a substituent group introduced into the base, wherein the substituent group is bound to the base via a triple bond. Novel nucleotide oligomers, nucleotide polymers, and nucleosides which can be used as raw materials or intermediates in the synthesis of this nucleotide oligomer and nucleotide polymer, as well as novel techniques for structural determination and manufacture of a functional substance having high affinity for a target, are provided.

Chemoselective N-deprotection of tert-butyl 2-(trifluoroacetylamino) esters under PTC conditions: Synthesis of tert-butyl 2-aminocarboxylates

Trifluoroacetamide 1 is alkylated in good yields (77-83%) by tert-butyl 2-bromocarboxylates 3 under solid-liquid phase transfer catalysis (PTC) conditions [anhydrous K2CO3, triethyl(benzyl)ammonium chloride (TEBA; 10%), MeCN, 80°C]. The resulting tert-butyl 2-(trifluoroacetylamino) carboxylates 5 are chemoselectively hydrolysed in 75-95% yields to the corresponding tert-butyl 2-amino carboxylates, isolated as hydrochlorides 8, under liquid-liquid PTC conditions [CH2Cl2 or Et2O, aqueous 20% KOH, TEBA (10%), 25-40°C].

Effect of N-trifluoroacetyl derivatives of amino acids and amino acid analogs on microbial antitumor screen

Eighteen trifluoroacetyl derivatives of amino acids and of amino acid analogs were prepared and tested for growth-inhibitory activity. Of the compounds tested, the trifluoroacetyl derivatives of o-, m-, and p-fluorophenylalanine and β-3-thienylalanine showed modest activity; trifluoroacetyl derivatives of phenylalanine and of β-2-thienylalanine showed marginal activity. The activity exhibited by the active trifluoroacetyl compounds was equal to that noted for most active chloroacetyl derivatives reported previously, as judged by comparison of their activity with that of chloroacetyl-m-fluorophenylalanine. No reversal of inhibition was noted when a representative of these inhibitors was challenged with a corresponding natural metabolite, both as free amino acid and as a noninhibitory acylated compound.