TY  - JOUR
A1  - Dai, Xiaolin
A1  - Böker, Alexander
A1  - Glebe, Ulrich
T1  - Broadening the scope of sortagging
JF  - RSC Advances
N2  - Sortases are enzymes occurring in the cell wall of Gram-positive bacteria. Sortase A (SrtA), the best studied sortase class, plays a key role in anchoring surface proteins with the recognition sequence LPXTG covalently to oligoglycine units of the bacterial cell wall. This unique transpeptidase activity renders SrtA attractive for various purposes and motivated researchers to study multiple in vivo and in vitro ligations in the last decades. This ligation technique is known as sortase-mediated ligation (SML) or sortagging and developed to a frequently used method in basic research. The advantages are manifold: extremely high substrate specificity, simple access to substrates and enzyme, robust nature and easy handling of sortase A. In addition to the ligation of two proteins or peptides, early studies already included at least one artificial (peptide equipped) substrate into sortagging reactions - which demonstrates the versatility and broad applicability of SML. Thus, SML is not only a biology-related technique, but has found prominence as a major interdisciplinary research tool. In this review, we provide an overview about the use of sortase A in interdisciplinary research, mainly for protein modification, synthesis of protein-polymer conjugates and immobilization of proteins on surfaces.
Y1  - 2019
U6  - https://doi.org/10.1039/c8ra06705h
SN  - 2046-2069
VL  - 9
IS  - 9
SP  - 4700
EP  - 4721
PB  - Royal Society of Chemistry
CY  - Cambridge
ER  -