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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
Statement of
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
RMID: 0020075690
DOI: 10.1021/jm061455n
Appears in Collections:Chemistry and Physics publications

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