Abstract
The structures of caspases reveal the mechanism of binding for non-peptide and protein inhibitors, and have been applied in the design of agents that either inhibit or activate caspases to control cell death in diverse diseases. Decreased cell death is desirable for treatment of stroke, nerve crush injury, myocardial infarction, neuromuscular and neurodegenerative diseases and several non-peptide caspase inhibitors have been developed. In contrast, activation of cell death would be advantageous in cancer therapy, and the strategy is to block the binding of inhibitory proteins to caspases. Recent preclinical studies are described.
Keywords: Cysteine protease, drug design, cell death, substrate recognition, apoptosis
Mini-Reviews in Medicinal Chemistry
Title: Caspases: Structure-Guided Design of Drugs to Control Cell Death
Volume: 8 Issue: 11
Author(s): Irene T. Weber, Bin Fang and Johnson Agniswamy
Affiliation:
Keywords: Cysteine protease, drug design, cell death, substrate recognition, apoptosis
Abstract: The structures of caspases reveal the mechanism of binding for non-peptide and protein inhibitors, and have been applied in the design of agents that either inhibit or activate caspases to control cell death in diverse diseases. Decreased cell death is desirable for treatment of stroke, nerve crush injury, myocardial infarction, neuromuscular and neurodegenerative diseases and several non-peptide caspase inhibitors have been developed. In contrast, activation of cell death would be advantageous in cancer therapy, and the strategy is to block the binding of inhibitory proteins to caspases. Recent preclinical studies are described.
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Cite this article as:
Weber T. Irene, Fang Bin and Agniswamy Johnson, Caspases: Structure-Guided Design of Drugs to Control Cell Death, Mini-Reviews in Medicinal Chemistry 2008; 8 (11) . https://dx.doi.org/10.2174/138955708785909899
DOI https://dx.doi.org/10.2174/138955708785909899 |
Print ISSN 1389-5575 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5607 |
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