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2011•Chemical CommunicationsRequires access

Enhancement of sortase A-mediated protein ligation by inducing a β-hairpin structure around the ligation site

Yûichi Yamamura, Hidehiko Hirakawa, Satoshi Yamaguchi, Teruyuki Nagamune

Open publisher page 65 citations

Abstract

A Staphylococcus aureus transpeptidase, sortase A (SrtA), catalyzes selective peptide/protein ligations that have been applied to cell imaging and protein engineering, while the ligations do not proceed to completion due to their reversibility. We successfully enhanced SrtA-mediated protein ligation through the formation of a β-hairpin around the ligation site.

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What this paper is about

A Staphylococcus aureus transpeptidase, sortase A (SrtA), catalyzes selective peptide/protein ligations that have been applied to cell imaging and protein engineering, while the ligations do not proceed to completion due to their reversibility. We successfully enhanced SrtA-mediated protein ligation through the formation of a β-hairpin around the ligation site.

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OpenAlex reports 65 citations for this work. Citation counts describe recorded attention and do not establish research quality.

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Available abstract

A Staphylococcus aureus transpeptidase, sortase A (SrtA), catalyzes selective peptide/protein ligations that have been applied to cell imaging and protein engineering, while the ligations do not proceed to completion due to their reversibility. We successfully enhanced SrtA-mediated protein ligation through the formation of a β-hairpin around the ligation site.

Key concepts: Sortase A, Ligation, Sortase, Chemical ligation, Chemistry, Peptide, Biophysics, Combinatorial chemistry

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