Polarization-dependent fluorescence of proteins bound to nanopore-confined lipid bilayers.
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.
Li
R-Q
RQ
Electronic Imaging Center at NJIT and ECE Department, NJIT, Newark, New Jersey 07102, USA.
Marek
A
A
Smirnov
Alex I
AI
Grebel
H
H
D001665:Binding Sites; D002627:Chemistry, Physical; D003198:Computer Simulation; D005453:Fluorescence; D008051:Lipid Bilayers / Q000737:chemistry*; D008956:Models, Chemical; D049329:Nanostructures / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D013997:Time Factors
D008051:Lipid Bilayers; D011506:Proteins