Issue 81, 2018
From the journal:

Chemical Communications

Directed sortase A evolution for efficient site-specific bioconjugations in organic co-solvents†

Zhi Zou,ab   Hoda Alibiglou,b   Diana M. Mate,‡a   Mehdi D. Davari,b   Felix Jakoba  and  Ulrich Schwaneberg ORCID logo *ab  

* Corresponding authors

a DWI – Leibniz Institute for Interactive Materials, Forckenbeckstraβe 50, 52056 Aachen, Germany

b Institute of Biotechnology, RWTH Aachen University, Worringerweg 3, 52074 Aachen, Germany
E-mail: u.schwaneberg@biotec.rwth-aachen.de

Abstract

Directed sortase A evolution yielded the variants R159G and D165Q/D186G/K196V with increased resistance (2.2-fold) and catalytic efficiency (6.3-fold) in 45% (v/v) dimethylsulfoxide. Interestingly, D165Q/D186G/K196V also showed an up to 4.7-fold increased activity for the conjugation of hydrophobic peptides/amines in co-solvents. MD simulations revealed that conformational mobilities are important for the gained resistance.

Graphical abstract: Directed sortase A evolution for efficient site-specific bioconjugations in organic co-solvents

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Article information

DOI
https://doi.org/10.1039/C8CC06017G
Article type
Communication
Submitted
24 Jul 2018
Accepted
19 Sep 2018
First published
20 Sep 2018

Chem. Commun., 2018,54, 11467-11470

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Directed sortase A evolution for efficient site-specific bioconjugations in organic co-solvents

Z. Zou, H. Alibiglou, D. M. Mate, M. D. Davari, F. Jakob and U. Schwaneberg, Chem. Commun., 2018, 54, 11467 DOI: 10.1039/C8CC06017G

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