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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.
Journal of Physical Chemistry B


electrochemical impedance spectroscopy, neutron reflectivity, phospholipase A2, tether bilayer membranes


Valincius, G. , McGillivray, D. , Febo-Ayala, W. , Ross, D. , Kasianowicz, J. and Losche, M. (2006), Enzyme Activity to Augment the Characterization of Tethered Bilayer Membranes, Journal of Physical Chemistry B (Accessed February 23, 2024)
Created June 1, 2006, Updated February 19, 2017