(659c) Using Phospholipase A2 to Create Air-Stable Supported Lipid Bilayers

Supported
lipid bilayer platform has a potential to be applied
as anti-biofouling surface and biosensor interface because
of the high bio-compatability and the ability to keep
biomolecule's orientation for specific ligand-receptor interaction. However, conventional
supported lipid bilayers may delaminate as they are exposed
to air-water interface, causing the difficulty in their long-term storage and
real-life application. Therefore, developing methods to maintain the integrity
and fluidity of lipid bilayers after dried and
rehydrated can significantly broaden the application. In this work, we observed
that a type of pheripheral enzyme, phosholipase A₂ (PLA₂), can induce
the formation of a branch-liked gel domain in the supported lipid bilayers. The branch-liked gel domains give aid to the
preservation of lipid bilayers when it is exposed to
air-water interface., The diffusivity of the
rehydrated lipid bilayers measured by the
fluorescence recovery after photobleaching technique was
found to be comparable to the one before dried, indicating that the fluidity of
the lipid bilayer is nearly unchanged. Our work
suggests that the gel domain induced by PLA₂ may play an important
role in the retention of supported lipid bilayers,
which leads to a new methodology of air-stable lipid bilayers
formation.