Quantitative analysis of protein-lipid interactions using tryptophan fluorescence.

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.

journal_name

Sci Signal

journal_title

Science signaling

authors

Kraft CA,Garrido JL,Leiva-Vega L,Romero G

doi

10.1126/scisignal.299pl4

subject

Has Abstract

pub_date

2009-12-01 00:00:00

pages

pl4

issue

99

eissn

1945-0877

issn

1937-9145

pii

scisignal.299pl4

journal_volume

2

pub_type

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