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.

引用

页数：7

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