22 March 2000 Time-resolved fluorescence measurements of actin-phalloidin interactions
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Proceedings Volume 3926, Advances in Nucleic Acid and Protein Analyses, Manipulation, and Sequencing; (2000) https://doi.org/10.1117/12.380519
Event: BiOS 2000 The International Symposium on Biomedical Optics, 2000, San Jose, CA, United States
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.
© (2000) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Michael K. Helms, Michael K. Helms, Todd E. French, Todd E. French, } "Time-resolved fluorescence measurements of actin-phalloidin interactions", Proc. SPIE 3926, Advances in Nucleic Acid and Protein Analyses, Manipulation, and Sequencing, (22 March 2000); doi: 10.1117/12.380519; https://doi.org/10.1117/12.380519
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