Quantitative Analysis of Protein-Lipid Interactions Using Tryptophan Fluorescence

Science Signaling  01 Dec 2009:
Vol. 2, Issue 99, pp. pl4
DOI: 10.1126/scisignal.299pl4

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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.

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