Phospholipid biotinylation of polydimethylsiloxane (PDMS) for protein immobilization.
Polydimethylsiloxane (PDMS) surfaces can be functionalized with biotin groups by adding biotinylated phospholipids to the PDMS prepolymer before curing. The addition of beta-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.
Huang
Bo
B
Department of Chemistry, Stanford University, Stanford, CA 94305-5080, USA.
Wu
Hongkai
H
Kim
Samuel
S
Kobilka
Brian K
BK
Zare
Richard N
RN
D001360:Avidin / Q000737:chemistry; D001710:Biotin / Q000737:chemistry / Q000502:physiology; D019921:Biotinylation; D004129:Dimethylpolysiloxanes / Q000737:chemistry*; D008954:Models, Biological; D015394:Molecular Structure; D010316:Particle Size; D010743:Phospholipids / Q000737:chemistry* / Q000502:physiology; D011506:Proteins / Q000737:chemistry* / Q000502:physiology; D012828:Silicones / Q000737:chemistry*; D013499:Surface Properties
D004129:Dimethylpolysiloxanes; D010743:Phospholipids; D011506:Proteins; D012828:Silicones; D001360:Avidin; C013830:baysilon; D001710:Biotin