Van Eyk, Dunn - Proteomic and Genomic Analysis of Cardiovascular Disease - 2003 (522919), страница 68
Текст из файла (страница 68)
These devices comprise a glass surface onto which a thinlayer of metal, usually gold, has been deposited and is subsequently covered by aself-assembled monolayer (SAM) of matrix such as carboxymethylated hydrogel[187], carboxymethylated dextran [188, 189] or a mixture of alkanethiolates [190,191]. The chemistry of the matrix is such that proteins and ligands may be immobilised on the sensor and when the target protein binds, the refractive index ofthe matrix changes.
The change in refractive index may be measured by a diodearray detector [190]. Clearly, if such devices could be made more parallel, i.e. witha larger number of protein recognition sites, and miniaturised they could possessconsiderable potential.Quartz crystal microbalance (QCM) devices are an interesting method for detecting antibody antigen interactions. In these, antibodies are bound to quartzcrystals through amino groups incorporated into ethylenediamine plasma-poly-14.6 Conclusionsmerised films [171].
The QCM is then exposed to the fluid to be analysed, binding of target antigen results in small changes in mass on the surface of the crystal and these changes are measured by detecting changes in resonance frequencyvia two gold electrodes. The sensitivity of these devices is such that they have thepotential to detect the interaction of a single protein molecule with a single antibody molecule.Other devices that have the potential to detect single molecule interactions include the force amplified biological sensor being developed by Colton and colleagues [192].
This is a modification of the atomic force microscope in which micron-sized magnetic particles are used in combination with micromachined piezoresistive cantilevers to measure antibody-antigen interactions. Finally, the possibility of incorporating biosensors into microelectronic circuits has been exploredusing molecular ion channels as sensing devices [193]. In this approach, a goldelectrode was attached to gramicidin molecules in the lower layer of a syntheticlipid membrane with the ion channel being formed by a second gramicidin molecule present in mobile form in the upper membrane layer. The mobile gramicidinmolecules were linked to an antibody such that binding of antigen to antibody altered the conductance properties of the channel.
There are many advantages offered by such a device, including the amplification that occurs as part of the detection event; thus, a single antigen-antibody interaction results in fluxes of millionsof ions per second (see [194]).14.6ConclusionsDespite the technical limitations associated with 2-DE, there is little doubt that, atpresent, it is unrivalled as a method to resolve up to several thousand proteins simultaneously (see [14]). Furthermore, the automation of at least part of the workflow from 2DE gels to protein identification has increased throughput and rapiddevelopments in the technology continue. It seems likely therefore that 2-DE andthese supporting techniques will remain in widespread use for some time yet.The technical limitations are sufficient to have motivated many to attempt to develop alternative methods of protein expression mapping.
We have reviewed someof these developments and in doing so, it has become evident that any futuretechnology for high-throughput protein expression analysis will almost certainlyrequire a multidisciplinary approach and the further development of novel methods. It remains to be seen whether the potential of ‘protein chips’ can be translated into an accessible, versatile and rigorous method for proteomic analyses.24524614 Protein Chip Technology14.7References1234567891011121314E. S.
Lander et al. ‘Initial sequencingand analysis of the human genome.’ Nature 2001, 409, 860–921.J. D. McPherson et al. ‘A physical mapof the human genome.’ Nature 2001,409, 934–941.J. C. Venter et al. ‘The sequence of thehuman genome.’ Science 2001, 291,1304–1351.M. Chee et al.
‘Accessing genetic information with high-density DNA arrays.’Science 1996, 274, 610–614.M. B Eisen, P. T. Spellman, P. O.Brown, D. Botstein. ‘Cluster analysisand display of genome-wide expressionpatterns.’ Proceedings of the NationalAcademy of Sciences of the United States ofAmerica 1998, 95, 14863–14868.D. Gerhold, T. Rushmore, C.
T. Caskey.‘DNA chips: promising toys have becomepowerful tools.’ Trends in BiochemicalScience 1999, 24, 168–173.S. Fields, O. Song. ‘A novel genetic system to detect protein-protein interactions.’ Nature 1989, 340, 245–246.M. Fromont-Racine, J. C. Rain, P. Legrain. ‘Toward a functional analysis ofthe yeast genome through exhaustivetwo-hybrid screens [see comments].’ Nature Genetics 1997, 16, 277–282.N. Lecrenier, F. Foury, A.
Goffeau.‘Two-hybrid systematic screening of theyeast proteome.’ Bioessays 1998, 20, 1–5.U. Scherf et al. ‘A gene expression database for the molecular pharmacology ofcancer.’ Nature Genetics 2000, 24, 236–244.T. Gaasterland, S. Bekiranov. ‘Makingthe most of microarray data.’ Nature Genetics 2000, 24, 204–206.D.
D. L. Bowtell. ‘Options available –from start to finish – for obtaining expression data by microarray.’ Nature Genetics 1999, 21, 25–32.K. M. Kurian, C. J. Watson, A. H. Wyllie. ‘DNA chip technology.’ Journal ofPathology 1999, 187, 267–271.A. Abbott. ‘A post-genomic challenge:learning to read patterns of protein synthesis.’ Nature 1999, 402, 715–720.15161718192021222323252627L. Anderson, J. Seilhamer.
‘A comparison of selected mRNA and protein abundances in human liver.’ Electrophoresis1997, 18, 533–537.N. L. Anderson, N. G. Anderson. ‘Proteome and proteomics: new technologies,new concepts, and new words.’ Electrophoresis 1998, 19, 1853–1861.W. P. Blackstock, M. P. Weir. ‘Proteomics: quantitative and physical mapping ofcellular proteins.’ Trends in Biotechnology1999, 17, 121–127.A. Dove.
‘Proteomics: translating genomics into products?’ Nature Biotechnology1999, 17, 233–236.R. Parekh. ‘Proteomics and molecularmedicine.’ Nature Biotechnology 1999, 17supplement, BV19–BV20.S. R. Pennington, M. R. Wilkins, D. F.Hochstrasser, M. J. Dunn. ‘Proteomeanalysis: from protein characterisation tobiological function.’ Trends in Cell Biology1997, 7, 168–173.M. R. Wilkins et al. ‘Progress with proteome projects: why all proteins expressed by a genome should be identified and how to do it.’ Biotechnology1995, 13, 19–50.S. M.
Dhanasekaran et al. ‘Delineationof prognostic biomarkers in prostate cancer.’ Nature 2001, 412, 822–826.A. T. Brünger. ‘X-ray crystallography andNMR reveal complementary views ofstructure and dynamics.’ Nature Structural Biology 1997, 4 Suppl, 862–865.S. Cusack et al. ‘Small is beautiful: protein micro-crystallography.’ Nature Structural Biology 1998, 5 Suppl, 634–637.M. Gerstein, H.
Hegyi. ‘Comparing genomes in terms of protein structure: surveys of a finite parts list.’ FEMS Microbiology Reviews 1998, 22, 277–304.B. Robson. ‘Beyond proteins.’ Trends inBiotechnology 1999, 17, 311–315.A. Sali, J. Kuriyan. ‘Challenges at thefrontiers of structural biology (Reprintedfrom Trends in Biochemical Science, vol12, Dec., 1999).’ Trends in Genetics 1999,15, M20–M24.14.7 References282930313233343536373839M. B Swindells, C. A. Orengo, D. T.Jones, E. G. Hutchinson, J. M. Thornton. ‘Contemporary approaches to protein structure classification.’ Bioessays1998, 20, 884–891.J.
P. Wery, R. W. Schevitz. ‘New trendsin macromolecular X-ray crystallography.’Current Opinion in Chemical Biology 1997,1, 365–369.E. M. Marcotte et al. ‘Detecting proteinfunction and protein-protein interactionsfrom genome sequences.’ Science 1999a,285, 751–753.E. M. Marcotte, M. Pellegrini, M. J.Thompson, T. O. Yeates, D. Eisenberg.‘A combined algorithm for genome-wideprediction of protein function.’ Nature1999b, 402, 83–86.P.
Bork et al. ‘Predicting function: fromgenes to genomes and back.’ Journal ofMolecular Biology 1998, 283, 707–725.M. Pellegrini, E. M. Marcotte, M. J.Thompson, D. Eisenberg, T. O. Yeates.‘Assigning protein functions by comparative genome analysis: protein phylogenetic profiles.’ Proceedings of the NationalAcademy of Sciences of the United States ofAmerica 1999, 96, 4285–4288.P. Uetz et al. ‘A comprehensive analysisof protein-protein interactions in Saccharomyces cerevisiae.’ Nature 2000, 403,623–627.A.
C. Gavin et al. ‘Functional organization of the yeast proteome by systematicanalysis of protein complexes.’ Nature2002, 415, 141–147.O. Puig et al. ‘The tandem affinity purification (TAP) method: A general procedure of protein complex purification.’Methods 2001, 24, 218–229.J. J. Tasto, R. H. Carnahan, W. H.McDonald, K. L. Gould. ‘Vectors andgene targeting modules for tandem affinity purification in Schizosaccharomycespombe.’ Yeast 2001, 18, 657–662.A. J. Enright, I.
Iliopoulos, N. C. Kyrpides, C. A. Ouzounis. ‘Protein interaction maps for complete genomes basedon gene fusion events.’ Nature 1999, 402,86–90.P. RossMacdonald et al. ‘Large-scaleanalysis of the yeast genome by transpo-40414243444546474849505152son tagging and gene disruption.’ Nature1999, 402, 413–418.A. H. Y.
Tong et al. ‘Systematic geneticanalysis with ordered arrays of yeast deletion mutants.’ Science 2001, 294, 2364–2368.P. James. ‘Protein identification in thepost-genome era: the rapid rise of proteomics.’ Quarterly Reviews of Physics 1997,30, 279–331.V. Santoni, M. Molloy, T. Rabilloud.‘Membrane proteins and proteomics: Unamour impossible?’ Electrophoresis 2000,21, 1054–1070.G. L. Corthals, V.
C. Wasinger, D. F.Hochstrasser, J. C. Sanchez. ‘The dynamic range of protein expression: Achallenge for proteomic research.’ Electrophoresis 2000, 21, 1104–1115.M. J. Dunn. ‘Quantitative two-dimensional gel electrophoresis: from proteinsto proteomes.’ Biochemical Society Transactions 1997, 25, 248–254.A. Gorg et al. ‘The current state of twodimensional electrophoresis with immobilized pH gradients.’ Electrophoresis2000, 21, 1037–1053.J. M. Hille, A. L. Freed, H. Watzig.‘Possibilities to improve automation,speed and precision of proteome analysis: A comparison of two-dimensionalelectrophoresis and alternatives.’ Electrophoresis 2001, 22, 4035–4052.H. J.
Issaq. ‘The role of separationscience in proteomics research.’ Electrophoresis 2001, 22, 3629–3638.S. E. Ong, A. Pandey. ‘An evaluation ofthe use of two-dimensional gel electrophoresis in proteomics.’ Biomolecular Engineering 2001, 18, 195–205.B. R. Herbert et al. ‘What place for polyacrylamide in proteomics?’ Trends in Biotechnology 2001, 19, S3–S9.J. Klose. ‘Large-Gel 2D Electrophoresis.’Methods in Molecular Biology 1999, 112:2–D Proteome Analysis Protocols, 147–172.J. E.
Celis et al. ‘Human and mouse proteomic databases: novel resources in theprotein universe.’ FEBS Letters 1998, 430,64–72.T. K. Chataway et al. ‘Development of atwo-dimensional gel electrophoresis data-24724814 Protein Chip Technology53545556575859606162base of human lysosomal proteins.’ Electrophoresis 1998, 19, 834–836.G.
![](https://s.studizba.com/z.php?f=/templates/si/i/noavatar.png&w=100&h=100&t=1"){kind=avatar}
