Enzyme activity to augment the characterization of tethered bilayer membranes.

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TitleEnzyme activity to augment the characterization of tethered bilayer membranes.
Publication TypeJournal Article
Year of Publication2006
AuthorsValincius, G, McGillivray, DJ, Febo-Ayala, W, Vanderah, DJ, Kasianowicz, JJ, Lösche, M
JournalJ Phys Chem B
Date Published2006 Jun 1
KeywordsLipid Bilayers, Models, Molecular, Phospholipases A, Phospholipases A2, Phospholipids

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.

Alternate JournalJ Phys Chem B
PubMed ID16722717
Grant List1 R01 1 RR14182 / RR / NCRR NIH HHS / United States