Significantly enhanced proteolytic activity of cyclen complexes by monoalkylationElectronic supplementary information (ESI) available: Experimental section, protein cleavage experiments, cytotoxicity studies, cmc determination. See DOI: 10.1039/c6dt00681g
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...
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Main Authors | , , , , , |
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Format | Journal Article |
Published |
28.06.2016
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Online Access | Get full text |
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Summary: | 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.
The activity of Cu(
ii
) and Co(
iii
) cyclen complexes in the cleavage of proteins was remarkably improved by introducing long alkyl chains thus generating efficient proteolytic amphiphilic metal complexes. |
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Bibliography: | Electronic supplementary information (ESI) available: Experimental section, protein cleavage experiments, cytotoxicity studies, cmc determination. See DOI 10.1039/c6dt00681g |
ISSN: | 1477-9226 1477-9234 |
DOI: | 10.1039/c6dt00681g |