Abstract
Sortase-mediated ligation is one of the most commonly used chemo-enzymatic techniques for the site-specific modification of proteins. We have established a new library of sortase mutants for directed evolution of sortase substrate selectivity. Phage display screens of this second-generation library yielded sortase mutants that ligate substrate proteins containing an APxTG or FPxTG recognition sequence instead of the canonical LPxTG sorting motif. These findings indicate that the second-generation sortase library is well suited for sortase engineering in order to increase the versatility of sortase-mediated ligation. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.
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