Abstract

The use of enzymes to catalyse peptide bond formation and for manipulating blocking groups during peptide synthesis is discussed. The history of solubility-controlled peptide condensations in the presence of proteolytic enzymes is traced. General techniques for obtaining improved yields of soluble condensation products are outlined along with special conditions which sometimes favour the enzymatic condensations of peptide fragments. Progress in the use of enzymes to manipulate blocking groups on α-amino groups, α-carboxyl groups, and on the sidechain functional groups of amino acid residues are examined. Some anticipated developments in the use of enzymes as reagents in peptide synthesis and semisynthesis are discussed.

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