title: Slide-format proteomic biochips based on surface-enhanced nanocluster-resonance.
abstract: The most fundamental properties of metal nanoclusters, namely the high local-field enhancement and nanoscale resonance behavior of the cluster electron plasma when exited by electromagnetic radiation, have been used to set up a variety of sensors transducing biorecognitive interactions into optical signals. This paper focuses on applications of resonant-cluster technology, which enabled us to monitor biorecognitive binding of a variety of proteins on a chip, thus constructing high-throughput interaction-screening devices. Decisive for this type of sensor is the nanometric distance from the local field surrounding a cluster to other parts of the sensor interacting with this field. In particular, the cluster-mirror or cluster-fluorophore distance gives rise to a variety of enhancement phenomena. Depending on the desired application this "resonance"- distance is approximately 5-400 nm. All types of sensor can be set up on photolithographically constructed microchips, but microscopic glass slides can also be employed; this also enables the use of standard devices for dotting and read out. Using slide based chips a standard format of 3,200 microdots (125 microm in diameter) was the basis of either microassays applying direct optical transduction via surfaceenhanced absorption or striking for more sensitivity via surface-enhanced fluorescence.
authors.affiliation: Institute of Analytical Biotechnology, Technical University Delft, The Netherlands. cm@kluyver.stm.tudelft.nl
authors.forename: C
authors.initials: C
authors.lastname: Mayer
authors.forename: N
authors.initials: N
authors.lastname: Stich
authors.forename: T
authors.initials: T
authors.lastname: Schalkhammer
authors.forename: G
authors.initials: G
authors.lastname: Bauer
mesh_terms: D000818:Animals; D004797:Enzyme-Linked Immunosorbent Assay / Q000295:instrumentation / Q000379:methods / Q000592:standards; D019085:Fluorescent Antibody Technique, Direct / Q000295:instrumentation / Q000379:methods; D006801:Humans; D007118:Immunoassay / Q000295:instrumentation / Q000379:methods / Q000592:standards; D008832:Microchemistry / Q000379:methods*; D020543:Proteome / Q000032:analysis*; D012680:Sensitivity and Specificity; D020349:Surface Plasmon Resonance / Q000379:methods*
chemical_list: D020543:Proteome