Development of lipopeptides for inhibiting 20S proteasomes

Bioorganic & Medicinal Chemistry Letters
Nicolas BasseRégis Vanderesse

Abstract

Proteasomes are responsible for the cytoplasmic turnover of the vast majority of proteins including regulatory proteins. We have synthesized lipopeptides a new class of non-covalent inhibitors of the 20S proteasome and assayed their inhibitory capacities. Their ability to inhibit at micromolar concentrations chymotrypsin-like and post-acid activities depends on peptide length (3 or 6 amino acids), sequence (presence of a positively or negatively charged amino acid), and alkyl chain length (C6-C18). These structural features could be varied to selectively inhibit one or more of the three proteasome activities.

Citations

Apr 4, 2013·Journal of Medicinal Chemistry·Sevil OzcanSaïd M Sebti
Dec 11, 2013·European Journal of Medicinal Chemistry·Makoto HasegawaTamio Mizukami
Mar 24, 2012·European Journal of Medicinal Chemistry·Xavier MaréchalJoëlle Vidal
Mar 4, 2014·Medicinal Research Reviews·Nicola MicaleMaria Zappalà
Dec 2, 2008·Bioorganic & Medicinal Chemistry Letters·Lucia FormicolaSandrine Ongeri
Nov 19, 2009·Journal of Medicinal Chemistry·Nicolas BasseMichèle Reboud-Ravaux
Oct 22, 2014·Journal of Medicinal Chemistry·Audrey DesvergneJoëlle Vidal
May 22, 2007·Journal of Medicinal Chemistry·Nicolas BasseJoëlle Vidal

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