Issue 26, 2016
From the journal:

Dalton Transactions

Significantly enhanced proteolytic activity of cyclen complexes by monoalkylation†

Chrischani Perera-Bobusch,a   Jan Hormann,a   Christoph Weise,b   Stefanie Wedepohl,cd   Jens Dernedded  and  Nora Kulak*a  

* Corresponding authors

a Institut für Chemie und Biochemie, Freie Universität Berlin, Fabeckstr. 34/36, 14195 Berlin, Germany
E-mail: nora.kulak@fu-berlin.de

b Institut für Chemie und Biochemie, Freie Universität Berlin, Thielallee 63, 14195 Berlin, Germany

c Institut für Chemie und Biochemie, Freie Universität Berlin, Takustr. 3, 14195 Berlin, Germany

d Charité – Universitätsmedizin Berlin, Institut für Laboratoriumsmedizin, Klinische Chemie und Pathobiochemie, CVK, Augustenburger Platz 1, 13353 Berlin, Germany

Abstract

A simple approach towards efficient artificial proteases based on the cyclen ligand is presented. We thus achieved an increase of the proteolytic activity of two orders of magnitude when compared to the unsubstituted cyclen complex. Amphiphilic Cu(II) and Co(III) complexes cut BSA and myoglobin as model substrates at μM concentrations. MALDI-ToF MS is used to identify the cleavage fragments.

Graphical abstract: Significantly enhanced proteolytic activity of cyclen complexes by monoalkylation

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Article information

DOI
https://doi.org/10.1039/C6DT00681G
Article type
Communication
Submitted
20 Feb 2016
Accepted
01 Jun 2016
First published
01 Jun 2016
This article is Open Access
Creative Commons BY license

Dalton Trans., 2016,45, 10500-10504

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Significantly enhanced proteolytic activity of cyclen complexes by monoalkylation

C. Perera-Bobusch, J. Hormann, C. Weise, S. Wedepohl, J. Dernedde and N. Kulak, Dalton Trans., 2016, 45, 10500 DOI: 10.1039/C6DT00681G

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