123253-85-0Relevant academic research and scientific papers
Kinetically Controlled Peptide Bond Formation in Anhydrous Alcohol Catalyzed by the Industrial Protease Alcalase
Chen, Shui-Tein,Chen, Shiah-Yun,Wang, Kung-Tsung
, p. 6960 - 6965 (2007/10/02)
The industrial alkaline protease alcalase has been found to be very stable (half life > 5 days in ethanol or 2-methyl-2-propanol) and active in alcoholic solvents (except methanol).Procedures have been developed for alcalase-catalyzed, kinetically controlled peptide bond formation in anhydrous alcohol (ethanol, 2-methyl-2-propanol).Studies of the selectivity of an alcalase-catalyzed reaction show that only L-amino acid acyl donors are substrates at the p-1 subsite of alcalase; at the p-1' subsite both D- and L-amino acid nucleophiles are substrates.Other amino compounds such as benzylamine and phenylhydrazine are good nucleophiles.Studies of the effect of the water content of the reaction solution on the yield in the synthesis of Moz-Phe-Leu-NH2 showed that the 95percent yield obtained in anhydrous 2-methyl-2-propanol was decreased to 48percent in 2-methyl-2-propanol containing 4.86percent water.
A Simple Method for Amide Formation from Protected Amino Acids and Peptides
Chen, Shui-Tein,Wu, Shih-Hsiung,Wang, Kung-Tsung
, p. 37 - 38 (2007/10/02)
Amide formation from protected amino acids and peptides is directly and simply achieved by using 1-hydroxybenzotriazole as activating agent and treating the intermediate O-(benzotriazol-1-yl) derivative ("active ester") in situ with 25percent ammonium hydroxide solution.
