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Issue 3, 2006
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Phospholipidbiotinylation of polydimethylsiloxane (PDMS) for protein immobilization

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Abstract

Polydimethylsiloxane (PDMS) surfaces can be functionalized with biotin groups by adding biotinylated phospholipids to the PDMS prepolymer before curing. The addition of β-D-dodecyl-N-maltoside (DDM) in the solution blocks non-specific protein binding on these functionalized PDMS surfaces. We characterize the surface by measuring fluorescently labeled streptavidin binding. Single molecule tracking shows that the phospholipids are not covalently linked to PDMS polymer chains, but the surface functionalization is not removed by washing. We demonstrate the immobilization of biotinylated antibodies and lectins through biotin–avidin interactions.

Graphical abstract: Phospholipid biotinylation of polydimethylsiloxane (PDMS) for protein immobilization

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Article information


Submitted
08 Nov 2005
Accepted
13 Jan 2006
First published
26 Jan 2006

Lab Chip, 2006,6, 369-373
Article type
Paper

Phospholipid biotinylation of polydimethylsiloxane (PDMS) for protein immobilization

B. Huang, H. Wu, S. Kim, B. K. Kobilka and R. N. Zare, Lab Chip, 2006, 6, 369
DOI: 10.1039/B515840K

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