Development of lipopeptides for inhibiting 20S proteasomes
Development of lipopeptides for inhibiting 20S proteasomes
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DOI：
10.1016/j.bmcl.2006.03.033
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发表时间：
2006-06-15
影响因子：
2.7
通讯作者：
Vanderesse, Rgis
中科院分区：
文献类型：
--
作者：
Basse, Nicolas;David, Papapostolou;Vanderesse, Rgis
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. (c) 2006 Elsevier Ltd. All rights reserved.
