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Flow‐Based Enzymatic Ligation by Sortase A
Author(s) -
Policarpo Rocco L.,
Kang Hansol,
Liao Xiaoli,
Rabideau Amy E.,
Simon Mark D.,
Pentelute Bradley L.
Publication year - 2014
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201403582
Subject(s) - sortase , sortase a , bioconjugation , chemistry , nucleophile , microreactor , flow chemistry , combinatorial chemistry , organic chemistry , biochemistry , bacterial protein , catalysis , gene
Sortase‐mediated ligation (sortagging) is a versatile, powerful strategy for protein modification. Because the sortase reaction reaches equilibrium, a large excess of polyglycine nucleophile is often employed to drive the reaction forward and suppress sortase‐mediated side reactions. A flow‐based sortagging platform employing immobilized sortase A within a microreactor was developed that permits efficient sortagging at low nucleophile concentrations. The platform was tested with several reaction partners and used to generate a protein bioconjugate inaccessible by solution‐phase batch sortagging.