Supramolecular architectures for the functionalization of solid surfaces.
Surface plasmon optical techniques are described as sensitive tools that allow for the on-line characterization of supramolecular biofunctional architectures at solid/solution interfaces. After a short introduction into the fundamentals of surface plasmon optics the observation of the build up of a functional bio-interface by the self-assembly process of long chain thiolates at an Au surface is described. Criteria are developed for tailoring the SAM architectures optimized for maximum protein binding from solution by specific bio-recognition reactions. SPM is employed to image the selective binding of streptavidin to a functionalized SAM laterally patterned by UV-photolithographic techniques.
Knoll
W
W
Max-Planck-Institut für Polymerforschung, Mainz, Germany.
Liley
M
M
Piscevic
D
D
Spinke
J
J
Tarlov
M J
MJ
D001426:Bacterial Proteins; D001710:Biotin; D008961:Models, Structural; D011485:Protein Binding; D011506:Proteins; D013057:Spectrum Analysis / Q000295:instrumentation / Q000379:methods*; D019809:Streptavidin; D013438:Sulfhydryl Compounds; D013499:Surface Properties
D001426:Bacterial Proteins; D011506:Proteins; D013438:Sulfhydryl Compounds; D001710:Biotin; D019809:Streptavidin