N-Terminal-prolonged vinyl ester-based peptides as selective proteasome beta 1 subunit inhibitors

The synthesis and biological properties of vinyl ester peptide-based molecules bearing linear N-terminal amino acids are reported. Compounds were tested in vitro for their capacity to inhibit the chymotryptic-, tryptic-like, and post-acidic activities of the proteasome. Some analogues showed selecti...

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Published in:Bioorganic & medicinal chemistry 2009-08, Vol.17 (15), p.5535-5540
Main Authors: Baldisserotto, Anna, Destro, Federica, Vertuani, Gianni, Marastoni, Mauro, Gavioli, Riccardo, Tomatis, Roberto
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container_end_page 5540
container_issue 15
container_start_page 5535
container_title Bioorganic & medicinal chemistry
container_volume 17
creator Baldisserotto, Anna
Destro, Federica
Vertuani, Gianni
Marastoni, Mauro
Gavioli, Riccardo
Tomatis, Roberto
description The synthesis and biological properties of vinyl ester peptide-based molecules bearing linear N-terminal amino acids are reported. Compounds were tested in vitro for their capacity to inhibit the chymotryptic-, tryptic-like, and post-acidic activities of the proteasome. Some analogues showed selective inhibition of post-acidic (PGPH) activity, which is attributed to the beta 1 subunit. Interestingly, active compounds demonstrated higher inhibitory activity toward 'standard' proteasomes than toward immunoproteasomes. The inhibitory potency was found to be related to the amino acidic sequence and to the length of the N-terminal residues. The new inhibitors demonstrated resistance to plasmatic proteases and a good capacity to permeate the cell membrane.
doi_str_mv 10.1016/j.bmc.2009.06.025
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title N-Terminal-prolonged vinyl ester-based peptides as selective proteasome beta 1 subunit inhibitors
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