%0 journal article
%@ 0022-2623
%A Abell, A.D.,Jones, M.A.,Neffe, A.T.,Aitken, S.G.,Cain, T.P.,Payne, R.J.,McNabb, S.B.,Coxon, J.M.,Stuart, B.G.,Pearson, D.,Lee, H.Y.-Y.,Morton, J.D.

%D 2007
%J Journal of Medicinal Chemistry
%N 12
%P 2916-2920 
%R doi:10.1021/jm061455n
%T Investigation into the P3 Binding Domain of m-Calpain Using Photoswitchable Diazo- and Triazene-dipeptide Aldehydes: New Anticataract Agents
%U https://doi.org/10.1021/jm061455n
12 
%X 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.