Cyclic peptidase substrates for fluorescent analysis of Caspase 3 enzyme activity

Anthony P. Guzikowski; Christina Shipp; Rachel A. Howard; Rod C. Schutte; Michael R. Braden; John J. Naleway

doi:10.1117/12.382040

11 April 2000 Cyclic peptidase substrates for fluorescent analysis of Caspase 3 enzyme activity

Anthony P. Guzikowski, Christina Shipp, Rachel A. Howard, Rod C. Schutte, Michael R. Braden, John J. Naleway

Proceedings Volume 3913, In-Vitro Diagnostic Instrumentation; (2000) https://doi.org/10.1117/12.382040
Event: BiOS 2000 The International Symposium on Biomedical Optics, 2000, San Jose, CA, United States

Abstract

Cyclic Caspase 3 peptidase substrates derived from the fluorophore Rhodamine 110, as well as their cleavage products, were prepared by step-wise synthesis, using three independent methods. 3D energy minimized structural analysis as well as Mass Spectral analysis indicate that the cyclic substrates can bind positively charged cations. Enzymatic assays indicate that the substrates are cleaved by the Caspase 3 enzyme. Cellular assays showed cell specific staining of apoptosis induced cell lines. Application of these substrates to the high-throughput screening analysis of apoptosis induction in whole cells was developed.

Citation Download Citation

Anthony P. Guzikowski, Christina Shipp, Rachel A. Howard, Rod C. Schutte, Michael R. Braden, and John J. Naleway "Cyclic peptidase substrates for fluorescent analysis of Caspase 3 enzyme activity", Proc. SPIE 3913, In-Vitro Diagnostic Instrumentation, (11 April 2000); https://doi.org/10.1117/12.382040

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