Development of lipopeptides for inhibiting 20S proteasomes
type: Dataset
description: 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
issued: 2026-05-05T16:20:19.401503
language: en
modified: 2026-05-05T16:20:19.401508
contact point: Organization
  fn: CCSD
keyword: infoeu-reposemanticsarticle
keyword: inhibitors
keyword: journal-articles
keyword: lipopeptides
keyword: proteasome
keyword: spigprocengineering-sciences-physicschemical-and-process-engineering
landing page: 0960-894X

Development of lipopeptides for inhibiting 20S proteasomes
type: Distribution
format: HTML
issued: 2026-05-05T16:20:19.402745
modified: 2026-05-05T16:20:19.393252
access URL: https://hal.science/hal-00097449

test_moissonnage_selune
type: Agent