Aspen Tree Protein SP1 as a Biological Nanopore

Michelle Akerman michelle.sykes@mail.huji.ac.il 1 Liron Nuttman 2 Maya Gofer 2 Dvir Rotem 1 Danny Porath 1 Oded Shoseyov 2
1Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem
2Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot

Nanopores have been used as stochastic sensors for the detection of analytes that range from small molecules to DNA, RNA, and proteins. Proteins in a planar lipid bilayer platform can be used as nanopores in order to study and identify these biological analytes. In this approach, individual analyte molecules modulate the ionic current flowing through a single nanopore. SP1 (stable protein 1) is a ring-shaped, highly stable homododecamer protein, originally isolated from Aspen trees (P. euphratica). SP1 is stable under extreme conditions such as high temperatures, detergents and organic solvents, and over a wide range of pH. SP1 has a relatively large pore diameter (3-4 nm) which can be manipulated in order to specifically detect a variety of analytes (DNA, RNA, Proteins). It was recently shown that SP1 can be embedded into lipid bilayers, thus creating a nanopore. The protein can be modified in order to change the charge distribution on its surface to further increase its stability in the lipid bilayer; this can be done via site directed mutagenesis and/or chemical modifications to increase surface hydrophobicity.

Michelle Akerman
Mrs. Michelle Akerman
Hebrew University of Jerusalem








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