Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/34465
Type: | Journal article |
Title: | Developments in the design and synthesis of calpain inhibitors |
Author: | Neffe, A. Abell, A. |
Citation: | Current Opinion in Drug Discovery and Development, 2005; 8(6):684-700 |
Publisher: | Current Drugs Ltd. |
Issue Date: | 2005 |
ISSN: | 1367-6733 2040-3437 |
Statement of Responsibility: | AT Neffe, AD Abell |
Abstract: | Calpains are Ca(2+)-dependent cysteine proteases that play an important role in cell differentiation and in apoptosis/necrosis. The overactivation of calpain is connected with a number of diseases, including cataracts and traumatic brain injury, making calpain an attractive drug target. The development of selective inhibitors of calpain has, however, proved difficult, due to a lack of detailed structural information on the protein. This difficulty has been somewhat alleviated with recent reports on the X-ray crystal structures of engineered calpains and improved biochemical characterization of the protein. This review describes properties and X-ray crystal structures of calpain, and the synthesis and binding affinities of novel calpain inhibitors. |
Keywords: | Aldehydes Amides Biphenyl Compounds Calpain Peptides Prodrugs Cysteine Proteinase Inhibitors Crystallography, X-Ray Inhibitory Concentration 50 Binding Sites Protein Conformation Drug Design Solubility |
Published version: | http://www.biomedcentral.com/1367-6733/8?issue=6 |
Appears in Collections: | Aurora harvest 6 Chemistry publications |
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.