Polarization-dependent fluorescence of proteins bound to nanopore-confined lipid bilayers

Document Type

Article

Publication Date

9-15-2008

Abstract

Lipid bilayers are essential structural component of biological membranes of all the living species: from viruses and bacteria to plants and humans. Biophysical and biochemical properties of such membranes are important for understanding physical mechanisms responsible for drug targeting. Binding events between proteins and the membrane may be ascertained by introducing fluorescence markers (chromophores) to the proteins. Here we describe a novel biosensing platform designed to enhance signals of these fluorescence markers. Nanoporous aluminum oxide membranes with and without gold (Au) surface coating have been employed for optical detection of bound conjugated streptavidin to biotinylated lipid bilayers-a model system that mimics protein docking to the membrane surface. Unexpectedly, it was found that fluorescence signals from such structures vary when pumped with E-polarized and H-polarized incident optical beams. The origin of the observed polarization-dependent effects and the implications for enhanced fluorescence detection in a biochip format are being discussed. © 2008 American Institute of Physics.

Identifier

51349146915 (Scopus)

Publication Title

Journal of Chemical Physics

External Full Text Location

https://doi.org/10.1063/1.2972143

ISSN

00219606

PubMed ID

19044890

Issue

9

Volume

129

Grant

IIS0514361

Fund Ref

National Science Foundation

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