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<p class="first" id="P1">Insertion of biological nanopore into artificial membrane
is of fundamental importance
in nanotechnology. Many applications require control and knowledge of channel orientation.
In this work, the insertion orientation of the bacteriophage SPP1 and phi29 DNA packaging
motor into lipid membranes was investigated. Single molecule electrophysiological
assays and Ni-NTA-nanogold binding assays revealed that both SPP1 and phi29 motor
channels exhibited a one-way traffic property for TAT peptide translocation from N-
to C-termini of the protein channels. SPP1 motor channels preferentially inserts into
liposomes with their C-terminal wider region facing inward. Changing the hydrophobicity
of the N- or C-termini of phi29 connector alters the insertion orientation, suggesting
that the hydrophobicity and hydrophilicity of the termini of the protein channel governs
the orientation of the insertion into lipid membrane. It is proposed that the specificity
in motor channel orientation is a result of the hydrophilic/hydrophobic interaction
at the air/water interface when the protein channels are incorporating into liposome