Quantitative Analysis of Protein-Lipid Interactions Using Tryptophan Fluorescence

被引：35
|
作者：
Kraft, Catherine A. [1 ]
Garrido, Jose Luis [1 ]
Leiva-Vega, Luis [1 ]
Romero, Guillermo [1 ]
机构：
[1] Univ Pittsburgh, Sch Med, Dept Pharmacol & Chem Biol, Pittsburgh, PA 15261 USA
来源：
SCIENCE SIGNALING | 2009年 / 2卷 / 99期
关键词：
PHOSPHATIDIC-ACID; RAF-1; KINASE; ULTRAVIOLET FLUORESCENCE; MEMBRANE TOPOLOGY; BINDING; INSERTION; TRANSLOCATION; ASSOCIATION; CHOLESTEROL; PEPTIDES;
D O I：
10.1126/scisignal.299pl4
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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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页数：7
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