title: Protein-detecting microarrays: current accomplishments and requirements.
abstract: The sequencing of the human genome has been successfully completed and offers the chance of obtaining a large amount of valuable information for understanding complex cellular events simply and rapidly in a single experiment. Interestingly, in addressing these proteomic studies, the importance of protein-detecting microarray technology is increasing. In the coming few years, microarray technology will become a significantly promising and indispensable research/diagnostic tool from just a speculative technology. It is clear that the protein-detecting microarray is supported by three independent but strongly related technologies (surface chemistry, detection methods, and capture agents). Firstly, a variety of surface-modification methodologies are now widely available and offer site-specific immobilization of capture agents onto surfaces in such a way as to keep the native conformation and activity. Secondly, sensitive and parallel detection apparatuses are being developed to provide highly engineered microarray platforms for simultaneous data acquisition. Lastly, in the development of capture agents, antibodies are now probably the most prominent capture agents for analyzing protein abundances. Alternative scaffolds, such as phage-displayed antibody and protein fragments, which provide the advantage of increasing diversity of proteinic capture agents, however, are under development. An approach involving recombinant proteins fused with affinity tag(s) and coupled with a highly engineered surface chemistry will provide simple production protocols and specific orientations of capture agents on the microarray formats. Peptides and other small molecules can be employed in screening highly potent ligands as well as in measuring enzymatic activities. Protein-detecting microarrays supported by the three key technologies should contribute in accelerating diagnostic/biological research and drug discovery.
authors.affiliation: Department of Bioengineering and The COE21 Program, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, B-40, 4259 Nagatsuta, Midori, Yokohama 226-8501, Japan.
authors.forename: Kin-ya
authors.initials: KY
authors.lastname: Tomizaki
authors.forename: Kenji
authors.initials: K
authors.lastname: Usui
authors.forename: Hisakazu
authors.initials: H
authors.lastname: Mihara
mesh_terms: D000818:Animals; D000906:Antibodies / Q000737:chemistry / Q000276:immunology; D006801:Humans; D046228:Microarray Analysis / Q000295:instrumentation / Q000379:methods; D009696:Nucleic Acids / Q000378:metabolism; D011108:Polymers / Q000737:chemistry; D040081:Protein Array Analysis / Q000295:instrumentation / Q000379:methods*; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D000906:Antibodies; D009696:Nucleic Acids; D011108:Polymers; D011506:Proteins