The mimics of N ε -acyl-lysine derived from cysteine as sirtuin inhibitors
| Autor: | Yongjun Li, Yan Li, Bin He, Xiaoxue Chen, Qingjie Zhao, Yefang Zou, Jingshan Shen, Fang Wang, Wang Chun, Hong Zhu |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
biology Chemistry Organic Chemistry Clinical Biochemistry Lysine Pharmaceutical Science Small Molecule Libraries SIRT2 Biochemistry Small molecule 03 medical and health sciences Inhibitory potency 030104 developmental biology Drug Discovery Sirtuin biology.protein Molecular Medicine Structure–activity relationship Molecular Biology Cysteine |
| Zdroj: | Bioorganic & Medicinal Chemistry Letters. 28:2375-2378 |
| ISSN: | 0960-894X |
| Popis: | Sirtuin inhibitors as physiological research tools and therapeutic potentials have caught many attentions in last decades. The mimics of acyl lysine have been approved to be a very efficient strategy for development of mechanism-based sirtuin inhibitors. In current study, a novel scaffold of l-S-(3-carboxamidopropyl) cysteine (l-CAPC) has been exploited for design and synthesis of sirtuin inhibitors. As a result, the mimics of Ne-acyl-lysine derived from cysteine including small molecules (5a-m) and peptides (9a-m) have been synthesized. Among these, the peptides 9g and 9h were found to be the most inhibitory potency and selectivity against SIRT2. |
| Databáze: | OpenAIRE |
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