Biomedical Engineering Reference
In-Depth Information
lows a wide range of applications that is unlimited by many of the constraints
traditionally associated with biological reagents. The acquisition of photoap-
tamers is limited only by the availability of individual proteins, and as that
repertoire and inventory increases the possibilities for photoaptamers will fol-
low closely behind.
The obvious ambition for protein microarray technology is to supplant the
laborious technologies now associated with proteomics: to make 2-D gel anal-
ysis and single-analyte ELISAs as obsolete for the study of protein expression
as Northern blots have become for the study of mRNA expression. Microar-
ray technology and its associated instrumentation are already cheaper, faster
and more-robust than the suite of technologies associated with 2-D gel/mass
spectrometry analysis. The acceptance of microarray technology for proteomic
analysis now awaits the introduction of assay platforms that are as sensitive
and comprehensive as the technologies we seek to replace.
The ideal microarray would combine the sensitivity of ELISA technol-
ogy with the comprehensive proteome coverage of 2-D gel/MS technology.
Antibody-based arrays have already shown impressive ELISA-like sensitivity
in small multiplex arrays [53,54]. However, the need to identify and apply sec-
ondary labelling antibodies will soon become an important constraint on the
degree of proteome coverage that can be achieved. Multiplexing with antibod-
ies may fall well short of the coverage provided by 2-D gels. Photoaptamers
start from a narrower technology base than do antibodies, but dispense with
the need for a secondary reagent. As the degree of multiplexing becomes more
critical in the development of protein microarray technology, the advantages
of a format based on a single capture and detection reagent will become more
important.
References
1. Guerrier-Takada, C., Gardiner, K. J., Marsh, T. L., Pace, N. R., and Altman, S.
(1983). The RNA Moiety Of RNase P Is The Catalytic Subunit Of The Enzyme .
Cell 35, 849-857
2. Kruger, K., Grabowski, P. J., Zaug, A. J., Sands, J., Gottschling, D. E., and
Cech, T. R. (1982). Self-splicing RNA: autoexcision and autocyclization of the
ribosomal RNA in-tervening sequence of Tetrahymena . Cell 31, 147-157
3. Beaucage, S. L., and Caruthers, M. H. (1981). Studies on Nucleotide Chemistry
V. Deoxynucleoside Phosphoramidites A New Class of Key Intermediates for
Deoxypolynucleotide Synthesis . Tetrahedron Lett 22, 1859
4. Matteucci, M. D., and Caruthers, M. H. (1981). Studies on Nucleotide Chemistry
IV. Synthesis of Deoxyoligonucleotides on a Polymer Support . J Am Chem Soc
103, 3185
5. Studier, F. W., and Moffatt, B. A. (1986). Use of bacteriophage T7 RNA poly-
merase to direct selective high-level expression of cloned genes . J Mol Biol 189,
113-130
6. Baltimore, D. (1970). RNA-dependent DNA polymerase in virions of RNA tu-
mour viruses . Nature 226, 1209-1211
Search WWH ::




Custom Search