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Proceedings Paper

Time-resolved fluorescence measurements of actin-phalloidin interactions
Author(s): Michael K. Helms; Todd E. French
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Paper Abstract

Compounds that interact with the cytoskeleton affect mobility and division, making them useful for treatment of certain types of cancer. Actin binding drugs such as the phallotoxins (small, bicyclic peptides) bind to and stabilize actin polymers (F-actin) without binding to actin monomers (G-actin). It has been shown that the intensity of fluorescently labeled phallotoxins such as fluorescein- phalloidin and rhodamine-phalloidin increases upon bind F- actin. We used LJL BioSystems' new FLAReTM technology to measure excited state lifetime changes of fluorescein- phalloidin and rhodamine-phalloidin upon binding to F- actin.

Paper Details

Date Published: 22 March 2000
PDF: 8 pages
Proc. SPIE 3926, Advances in Nucleic Acid and Protein Analyses, Manipulation, and Sequencing, (22 March 2000); doi: 10.1117/12.380519
Show Author Affiliations
Michael K. Helms, LJL BioSystems, Inc. (United States)
Todd E. French, LJL BioSystems, Inc. (United States)


Published in SPIE Proceedings Vol. 3926:
Advances in Nucleic Acid and Protein Analyses, Manipulation, and Sequencing
Patrick A. Limbach; John C. Owicki; Ramesh Raghavachari; Weihong Tan, Editor(s)

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