Citation
Xia, Nan; Shumaker-Parry, Jennifer S.; Zareie, M. Hadi; Campbell, Charles T.; & Castner, David G. (2004).
A Streptavidin Linker Layer That Functions after Drying.
Langmuir, 20(9), 3710-3716.
Abstract
The ability of streptavidin (SA) to simultaneously bind four biotins is often used in linker layers, where a biotinylated molecule is linked to a biotin-functionalized surface via SA. For biosensor and array applications, it is desirable that the SA linker layer be stable to drying and rehydration. In this study it was observed that a significant decrease in binding capacity of a SA layer occurred when that layer was dried. For this study a SA linker layer was constructed by binding SA to a biotin-containing alkylthiolate monolayer (BAT/OEG) self-assembled onto gold. Its stability after drying was investigated using surface plasmon resonance (SPR). Approximately a quarter of the SA layer was removed from the BAT/OEG surface upon drying and rehydration, suggesting disruption of SA?biotin binding when dry. This resulted in the dried SA layer losing ?40% of its biotinylated ferritin (BF) binding capacity. Coating the layer with trehalose before drying was found to inhibit the loss of SA from the BAT/OEG surface. SPR showed that the trehalose-protected SA linker layer retained ?91% of its original BF binding capacity after drying and rehydration. Atomic force microscopy, which was used to image individual surface-bound SA and BF molecules, qualitatively confirmed these observations.
Reference Type
Journal Article
Secondary Title
Langmuir
Author(s)
Xia, NanShumaker-Parry, Jennifer S.Zareie, M. HadiCampbell, Charles T.Castner, David G.
Year Published
2004
Date Published
1080777600
Volume Number
20
Issue Number
9
Pages
3710-3716
DOI
10.1021/la035864n
