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Proceedings Paper

Cyclic peptidase substrates for fluorescent analysis of Caspase 3 enzyme activity
Author(s): Anthony P. Guzikowski; Christina Shipp; Rachel A. Howard; Rod C. Schutte; Michael R. Braden; John J. Naleway
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Paper 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.

Paper Details

Date Published: 11 April 2000
PDF: 10 pages
Proc. SPIE 3913, In-Vitro Diagnostic Instrumentation, (11 April 2000); doi: 10.1117/12.382040
Show Author Affiliations
Anthony P. Guzikowski, Marker Gene Technologies, Inc. (United States)
Christina Shipp, Marker Gene Technologies, Inc. (United States)
Rachel A. Howard, Marker Gene Technologies, Inc. (United States)
Rod C. Schutte, Marker Gene Technologies, Inc. (United States)
Michael R. Braden, Marker Gene Technologies, Inc. (United States)
John J. Naleway, Marker Gene Technologies, Inc. (United States)


Published in SPIE Proceedings Vol. 3913:
In-Vitro Diagnostic Instrumentation
Gerald E. Cohn, Editor(s)

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