Quantitative Analysis of Protein-Lipid Interactions Using Tryptophan Fluorescence
- 1 December 2009
- journal article
- protocols
- Published by American Association for the Advancement of Science (AAAS) in Science Signaling
- Vol. 2 (99), pl4
- https://doi.org/10.1126/scisignal.299pl4
Abstract
The fluorescent properties of the amino acid tryptophan make it a useful tool for fluorometric assays. Because tryptophan fluorescence is remarkably sensitive to the polarity of the environment, it can be used to determine the affinity of tryptophan-containing peptides for phospholipid vesicles of varying compositions. Here, we describe a method for using tryptophan fluorescence to determine the binding affinities of peptides derived from the proteins Raf-1 and KSR-1 to small unilamellar vesicles containing phosphatidic acid. The method can be extrapolated to measure the binding of other tryptophan-containing peptides or proteins to lipid vesicles.Keywords
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