Localized Surface Plasmon Resonance Sensing of Lipid-Membrane-Mediated Biorecognition Events
Supported phospholipid bilayers (SPBs) have emerged as important model systems for studies of the natural cell membrane and its components, which are essential for the integrity and function of cells in all living organisms, and also constitute common targets for therapeutic drugs and in disease dia...
Saved in:
Published in | Journal of the American Chemical Society Vol. 127; no. 14; pp. 5043 - 5048 |
---|---|
Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Washington, DC
American Chemical Society
13.04.2005
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | Supported phospholipid bilayers (SPBs) have emerged as important model systems for studies of the natural cell membrane and its components, which are essential for the integrity and function of cells in all living organisms, and also constitute common targets for therapeutic drugs and in disease diagnosis. However, the preferential occurrence of spontaneous SPB formation on silicon-based substrates, but not on bare noble-metal surfaces, has so far excluded the use of the localized surface plasmon resonance (LSPR) sensing principle for studies of lipid-membrane-mediated biorecognition reactions. This is because the LSPR phenomenon is associated with, and strongly confined to, the interfacial region of nanometric noble-metal particles. This problem has been overcome in this study by a self-assembly process utilizing localized rupture of phospholipid vesicles on silicon dioxide in the bottom of nanometric holes in a thin gold film. The hole-induced localization of the LSPR field to the voids of the holes is demonstrated to provide an extension of the LSPR sensing concept to studies of reactions confined exclusively to SPB-patches supported on SiO2. In particular, we emphasize the possibility of performing label-free studies of lipid-membrane-mediated reaction kinetics, including the compatibility of the assay with array-based reading (∼7 × 7 μm2) and detection of signals originating from bound protein in the zeptomole regime. |
---|---|
Bibliography: | istex:C132CBD826E8656F4EE077C949E567709635D47B ark:/67375/TPS-WMVZ9LG4-1 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0002-7863 1520-5126 1520-5126 |
DOI: | 10.1021/ja043672o |