The high selectivity and the mild reaction conditions of enzymatic processes prompted their application in the synthesis of peptides, where selectivity is a feature of pivotal importance. Here we report the use of the serine protease subtilisin for the selective deprotection of C-terminal tert-butyl esters, achieved in good to quantitative yield for most of the natural amino acids. The same enzyme was active in the C-terminal amidation affording excellent yields with several peptides in the presence of a variety of amino sources. Subtilisin, finally, can also catalyse the transesterification of C-terminal primary esters. All the reactions are highly selective and neither side chains modifications nor N-terminus reactions have been observed. The endopeptidase activity, an important drawback in the use of proteases, was minimized upon extensive optimization of the reaction conditions.
There are no comments yet. You can post the first one!
Post a comment
Please log in to use this service. Login as Wageningen University & Research user or guest user in upper right hand corner of this page.