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Issue 53, 2020
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Trivalent metal complex geometry of the substrate governs cathepsin B enzymatic cleavage rate

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Abstract

The lysosomal protease cathepsin B recognizes defined, short peptide sequences, providing means for effective, targeted drug release. Here, we show that the introduction of a coordination complex adjacent to the cleavage sequence allows us to tune enzymatic cleavage rate by varying the complexed, trivalent metal ion.

Graphical abstract: Trivalent metal complex geometry of the substrate governs cathepsin B enzymatic cleavage rate

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Supplementary files

Article information


Submitted
20 Apr 2020
Accepted
26 May 2020
First published
26 May 2020

Chem. Commun., 2020,56, 7289-7292
Article type
Communication

Trivalent metal complex geometry of the substrate governs cathepsin B enzymatic cleavage rate

S. H. Ahn, J. N. Iuliano and E. Boros, Chem. Commun., 2020, 56, 7289
DOI: 10.1039/D0CC02862B

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