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Recent Advances in the Development of Legumain-selective Chemical Probes and Peptide Prodrugs by Marcin Poreba is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Recent Advances in the Development of Legumain-selective Chemical Probes and Peptide Prodrugs about?

Legumain, which is also known as vacuolar processing enzyme (VPE) or asparaginyl endopeptidase (AEP), is a cysteine protease that was first discovered and characterized in the leguminous seeds of the moth bean in the early 1990s. Later, this enzyme was also detected in higher organisms, including eukaryotes. This pH-dependent protease displays the highest activity in acidic endolysosomal compartments; however, legumain also displays nuclear, cytosolic and extracellular activity when stabilized by other proteins or intramolecular complexes. Based on the results from over 25 years of research, this protease is involved in multiple cellular events, including protein degradation and antigen presentation. Moreover, when dysregulated, this protease contributes to the progression of several diseases, with cancer being the well-studied example. Research on legumain biology was undoubtedly facilitated by the use of small molecule chemical tools. Therefore, in this review, I present the historical perspectives and most current strategies for the development of small molecule substrates, inhibitors and activity-based probes for legumain. These tools are of paramount importance in elucidating

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Author

Marcin Poreba

Publisher

Walter de Gruyter GmbH & Co. KG; Walter de Gruyter GmbH (ISSN 1431-6730)

Published

2019

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)