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https://hdl.handle.net/2440/42094
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Type: | Journal article |
Title: | Investigation into the P3 binding domain of m-calpain using photoswitchable diazo- and triazene-dipeptide aldehydes: New anticataract agents |
Author: | Abell, A. Jones, M. Neffe, A. Aitken, S. Cain, T. Payne, R. McNabb, S. Coxon, J. Stuart, B. Pearson, D. Lee, H. Morton, J. |
Citation: | Journal of Medicinal Chemistry, 2007; 50(12):2916-2920 |
Publisher: | Amer Chemical Soc |
Issue Date: | 2007 |
ISSN: | 0022-2623 1520-4804 |
Statement of Responsibility: | Andrew D. Abell, Matthew A. Jones, Axel T. Neffe, Steven G. Aitken, Thomas P. Cain, Richard J. Payne, Stephen B. McNabb, James M. Coxon, Blair G. Stuart, David Pearson, Hannah Y.-Y. Lee, and James D. Morton |
Abstract: | The photoswitchable N-terminal diazo and triazene-dipeptide aldehydes 8a-d, 10a,b, and 17a,b present predominantly as the (E)-isomer, which purportedly binds deep in the S3 pocket of calpain. All compounds are potent inhibitors of m-calpain, with 8b being the most active (IC50 of 35 nM). The diazo-containing inhibitors 8a, 8c, and 10a were irradiated at 340 nm to give a photostationary state enriched in the (Z)-isomer, and in all cases, these were less active. The most water soluble triazene 17a (IC50 of 90 nM) retards calpain-induced cataract formation in lens culture. |
Keywords: | Lens, Crystalline Animals Sheep Humans Cataract Aldehydes Sulfonamides Azo Compounds Triazenes Calpain Dipeptides Culture Techniques Ultraviolet Rays Protein Structure, Tertiary Protein Binding Structure-Activity Relationship Stereoisomerism Models, Molecular |
Rights: | Copyright © 2007 American Chemical Society |
DOI: | 10.1021/jm061455n |
Published version: | http://dx.doi.org/10.1021/jm061455n |
Appears in Collections: | Aurora harvest Chemistry and Physics publications |
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