Abstract
The coupling between the carbamoylmethyl ester of an N-protected amino acid or dipeptide (at 25 mM) and an amino acid amide (at 100 mM) was achieved using Aspergillus melleus protease in 1,1,1,3,3,3-hexafluoro-2-propanol/N,N-dimethylformamide (1:1, v/v); the coupling efficiencies were dependent largely on the combination of amino acid residues: e.g. the dipeptide yields after 48 h were for l-Ala + Gly, ∼100% and for l-Leu + l-Leu, 16%.
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Miyazawa, T., Hiramatsu, M., Murashima, T. et al. Aspergillus melleus protease-catalyzed peptide synthesis using the carbamoylmethyl ester as an acyl donor in 1,1,1,3,3,3-hexafluoro- 2-propanol/N,N-dimethylformamide. Biotechnology Letters 24, 1945–1949 (2002). https://doi.org/10.1023/A:1021121631031
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DOI: https://doi.org/10.1023/A:1021121631031