Enzyme activity to augment the characterization of tethered bilayer membranes

被引：68
作者：
Valincius, Gintaras
McGillivray, Duncan J.
Febo-Ayala, Wilma
Vanderah, David J. [1 ]
Kasianowicz, John J.
Losche, Mathias
机构：
[1] NIST, Div Biochem Sci, Gaithersburg, MD 20899 USA
[2] Inst Biochem, LT-08662 Vilnius, Lithuania
[3] NIST, NCNR, Gaithersburg, MD 20899 USA
[4] Carnegie Mellon Univ, Dept Phys, Pittsburgh, PA 15213 USA
[5] NIST, Div Semicond Elect, Gaithersburg, MD 20899 USA
来源：
JOURNAL OF PHYSICAL CHEMISTRY B | 2006年 / 110卷 / 21期
关键词：
D O I：
10.1021/jp0616516
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
The rate of Ca2+-triggered phospholipase A(2) (PLA(2)) degradation of tethered bilayer membranes (tBLMs), composed of a synthetic lipid, beta-mercaptoethanol, and palmitoyloleoylphosphatidylcholine (POPC), is similar to 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 PLA(2) is a sensitive probe of short length scale structural differences not revealed by EIS and NR.
引用
收藏
页码：10213 / 10216
页数：4
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