Enzyme activity to augment the characterization of tethered bilayer membranes.
The rate of Ca2+ -triggered phospholipase A2 (PLA2) degradation of tethered bilayer membranes (tBLMs), composed of a synthetic lipid, beta-mercaptoethanol, and palmitoyloleoylphosphatidylcholine (POPC), is approximately 80 times greater than for those prepared with diphytanoylphosphatidylcholine (DPhyPC). Electrochemical impedance spectroscopy (EIS) and neutron reflectivity (NR) data indicate complete, water-free tBLMs that exhibit near ideal capacitive behavior and the presence of a water reservoir in the bilayer subspace proximal to the substrate (Au) surface for both tBLMs. Together these data indicate that the POPC and the DPhyPC tBLMs are structurally similar along the surface normal but markedly different at the outer leaflet/solution interface and that PLA2 is a sensitive probe of short length scale structural differences not revealed by EIS and NR.
Valincius
Gintaras
G
McGillivray
Duncan J
DJ
Febo-Ayala
Wilma
W
Vanderah
David J
DJ
Kasianowicz
John J
JJ
Lösche
Mathias
M
D008051:Lipid Bilayers; D008958:Models, Molecular; D010741:Phospholipases A / Q000737:chemistry / Q000378:metabolism*; D054467:Phospholipases A2; D010743:Phospholipids / Q000737:chemistry*
D008051:Lipid Bilayers; D010743:Phospholipids; D010741:Phospholipases A; D054467:Phospholipases A2