Abstract
The proteasome is a multicatalytic protease responsible for the degradation of misfolded proteins. We have synthesized fluorogenic substrates in which the peptide chain was systematically elongated from two to six amino acids and evaluated the effect of peptide length on all three catalytic activities of human 20S proteasome. In the cases of five- and six-membered peptides, we have also synthesized libraries of fluorogenic substrates. Kinetic analysis revealed that six-amino-acid substrates are significantly better for chymotrypsin-like and caspase-like activity than shorter peptidic substrates. In the case of trypsin-like activity, a five-amino-acid substrate was optimal.
Acknowledgments
This research was supported by the State for Scientific Research in Poland and the Foundation for Polish Science (Grant/Award Number: ‘FOCUS’). This project was supported by the Wroclaw Centre of Biotechnology, a program of The Leading National Research Centre (KNOW), for the years 2014–2018.
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Supplemental Material:
The online version of this article (DOI: 10.1515/hsz-2016-0176) offers supplementary material, available to authorized users.
©2016 Walter de Gruyter GmbH, Berlin/Boston
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- Frontmatter
- Guest Editorial
- Highlight: proteolytic networks across cellular boundaries
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- A personal journey with matrix metalloproteinases
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