Enzyme Activity to Augment the Characterization of Tethered Bilayer Membranes
Gintaras Valincius, Duncan J. McGillivray, W. Febo-Ayala, David J. Vanderah, John J. Kasianowicz, Mathias Losche
The structural order of tethered lipid bilayers (tBLMs) on solid substrates, investigated with electrochemical impedance spectroscopy (EIS) and neutron reflectivity (NR), is further characterized by phospholipase activity. Whereas EIS and NR data indicate tBLMs with complete and coherent bilayer structures possessing ideal capacive behavior, phospholipase activity on the palmitoyloleoylphosphatidylcholine (POPC) tBLMs is ~ 2 orders of magnitude larger than on the diphytanoylphosphatidylcholine (DPhPC) tBLMs. These data show that phospholipase activity is a sensitive amplifier of defect states within local order of the bilayer structure.
, McGillivray, D.
, Febo-Ayala, W.
, Ross, D.
, Kasianowicz, J.
and Losche, M.
Enzyme Activity to Augment the Characterization of Tethered Bilayer Membranes, Journal of Physical Chemistry B
(Accessed June 4, 2023)