31677-20-0Relevant academic research and scientific papers
Synthesis of an enantiopure thioester as key substrate for screening the sensitivity of penicillin binding proteins to inhibitors
Simon, Justine F.,Bouillez, André,Frère, Jean-Marie,Luxen, André,Zervosen, Astrid
, p. 22 - 31 (2016/10/31)
The synthesis of the enantiopure thioester (R)-2-(2-benzamidopropanoylthio)acetic acid was developed. After the exploration of several activation methods, reaction conditions were found for the formation of the thioester bond in the presence of propylphosphonic anhydride with high enantioselectivity (ee > 99%). The thioester activity of Penicillin Binding Proteins is helpful in research programs looking for new lead structures to overcome the problem of bacterial resistance.
DIISOPROPYLETHYLAMINE ELIMINATES DIPEPTIDE FORMATION DURING THE ACYLATION OF AMINO ACIDS USING BENZOYL CHLORIDE AND SOME ALKYL CHLOROFORMATES
Chen, Francis M. F.,Benoiton, N. Leo
, p. 1224 - 1227 (2007/10/02)
Acylation of amino acids using benzoyl chloride in aqueous alkali leads to benzoylamino acids containing one percent of benzoyldipeptide.Use of diisopropylethylamine instead of sodium hydroxide as base eliminates the side reaction responsible for the contaminant.Ethoxycarbonylamino acids are advantageously prepared in the same manner using ethyl chloroformate or diethyl dicarbonate.The latter gives rise to some N-substituted dipeptide when used in aqueous alkali.The method is unsatisfactory for the benzyloxycarbonylation of amino acids.Use of 9-fluorenylmethyl chloroformate and diisopropylethylamine gives the pure derivative of leucine in moderate yield.
