The ability of microbial transglutaminase to ligate two polypeptides through glutamine and lysine residues was exploited to generate cyclic peptides. Peptides with an N-terminal short glutamine-donor sequence (Ala-Leu-Gln), a variable polypeptide linker and a C-terminal lysine residue could efficiently be cyclised by the enzyme.
Enzymatic Cyclisation of Peptides with a Transglutaminase
ANGELINI, Alessandro;
2011-01-01
Abstract
The ability of microbial transglutaminase to ligate two polypeptides through glutamine and lysine residues was exploited to generate cyclic peptides. Peptides with an N-terminal short glutamine-donor sequence (Ala-Leu-Gln), a variable polypeptide linker and a C-terminal lysine residue could efficiently be cyclised by the enzyme.
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