Fluorescence assays for screening combinatorial libraries of drug candidates

Current Opinion in Drug Discovery and Development

Volumn 1, Issue 1, 1998, Pages 98-105

  Finney, Nathaniel S ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

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[No Author keywords available]

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EID: 0012155954     PISSN: 13676733     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (31)

1. A Practical Guide to Combinatorial Chemistry. Czamik AW, DeWitt SH (Eds): American Chemical Society, Washington, DC, 1997.
2. Combinatorial Chemistry - Synthesis and Application. Wilson SR, Czamik AW (Eds): John Wiiey & Sons, New York, 1997.
3. Combinatorial Peptide and Nonpeptide Libraries. Jung G (Ed):VCH, New York, 1996. References [1,2,3] are the edited texts currently available covering combinatorial chemistry and solid phase synthesis. There are numerous excellent reviews articles available as well, almost all of which are cited in these books.
4. Craig, FF: Screening of combinatorial libraries. In: A Practical Guide to Combinatorial Chemistry. Czamik AW, DeWitt SH (Eds): American Chemical Society, Washington, DC, (1997):399-412. This is a good overview of the current state of high-throughput screening. While it focuses almost exclusively on fluorescent and radioactivity-based assays, it does an excellent job of describing the relevant abstract concerns.
5. Burbaum JJ, Sigal NH: New technologies for high-throughput screening. CurrOpin Chem B/b/(1997) 1:72-78. A shorter, but technologically broader, supplement to reference [4].
6. Rogers MV: Light on high-throughput screening: Fluorescence-based assay technologies. Drug Disc Today (1997) 2:156-160. A thorough overview of the technical aspects (in terms of hardware and methodology) of the most common fluorescence-based approaches to high-throughput screening.
7. Cubitt AB, Heim R, Adams SR, Boyd AE, Grass LA, Tsien RY: Understanding, improving and using green fluorescent proteins. TIBS (1995) 20:448-455. This remains one of the best overviews of GFP applications, outlining the most important emission-modulating mutations, as well as extensive unpublished early efforts in cellular GFP expression.
8. Misteii T, Spector DL: Applications of the green fluorescent protein in cell biology and biotechnology. Nature Blotech (1997) 15:961 -964. A newer review which, while not as extensive as that of Cubitt et al, contains lead references to the important developments after 1995.
9. Ormo M, Cubitl AB, Kallio K, Gross LA, Tsien RY, Remington SJ: Crystal structure of the Aequorea Victoria green fluorescent protein. Science (1996) 273:1392-1395. A remarkable paper which discloses not only the high-resolution X-ray structure of the protein, but also several new color mutants of GFP that are not included in reference [11]. It includes a discussion of the design rationale for the point-mutated color variants.
10. Yang F, Moss LG, Phillips GN: The molecular structure of green fluorescent protein. Nature Biotech (1996) 14:1246-1251. A parallel report of the GFP X-ray structure.
11. Heim R, Tsien RY: Engineering green fluorescent protein for Improved brightness, longer wavelengths and fluorescence resonance energy transfer. Curr Bio/(1996) 6:178-82. A thorough discussion of the basic fluorescent properties of the protein, accompanied by a discussion of several important color mutants developed by the authors.
12. Cormack BP, Valdivia RH, Falkow S: FACS-optimized mutants of the green fluorescent protein (GFP). Gene (1996)173:33-38. This paper not only reports a bright GFP mutant, but demonstrates the use of fluorescence-activated cell sorting (FACS) with GFP. (In fact, FACS was used to isolate the bright mutants from large collections of cells.)
13. Rizzuto R, Brini M, De Giorgi F, Rossi R, Heim R, Tsien RY, Pozzan T: Double labeling of subcellular structures with organelle-targeted GFP mutants in vivo. Current Biology (1996)6:183-8. This work reports the use of GFP with a widely-used human cell line (HeLa cells). It also reports the expression and simultaneous detection of two GFP color-mutants, setting the stage for the study of protein-protein interactions by double-labeling.
14. Muldoon RR, Levy JP, Kain SR, Kitts PA, Link CJ: Tracking and quantitation of retroviral-mediated transfer using a completely humanized, red-shifted green fluorescent protein gene. Biotechniques (1997) 22:162-167. The authors demonstrate the retroviral Insertion of a humanized gene from a commercial source, and show that GFP fluorescence can be used as a quantitative measure of gene expression.
15. Chiocchetti A, Tolosano E, Hirsch E, Silengo L, Altruda F: Green fluorescent protein as a reporter of gene expression in transgenic mice. Biochem Biophys Acta (1997) 1352:193-202. A recent demonstration that GFP-labeled mouse cells can be used in whole-organism applications. The work includes a thorough comparison of the use of GFP and LacZ reporter genes for several applications.
16. Okabe M, Ikawa M, Kominami K, Nakanishi T, Nishimune Y: 'Green mice1 as a source of ubiquitous green cells. FEBS Letters (1997) 407:313-9. In perhaps the most convincing demonstration that GFP is not necessarily toxic to mammalian cells, the authors report the accidental development or a strain of completely fluorescent hairless mice. Color photographs may be perused, among other places, at httptfwww.popsci.eom/content/science/news/971206.s.html
17. Femandez-Abalos JM, Fox H, Pitt C, Wells B, Doonan JH: Plant-adapted green fluorescent protein is a versatile vital reporter for gene expression, protein localization and mitosis in the filamentous fungus, Aspergillus nidulans. Mol Microbiol (1998) 27:121 -130. A recent report of high-le vel expression in a popular fungal cell line, which is particularly impressive in that WT GFP generally does not express weII in fungi.
18. Cormack BP, Bertram G, Egerton M, Gow NAR, Falkow S, Brown AJP: Yeast-enhanced green fluorescent protein (yEGFP): A reporter of gene expression in Candida albicans. Microbiol (1997) 143:303-311.
19. Morschhauser J, Michel S, Hacker J: Expression of a chromosomally integrated, single-copy GFP gene in Candida albicans, and its use as a reporter of gene regulation. Molecular & General Genetics (1998) 257:412-420. Similar to the report with Aspergillus above, the authors of these papers have re-engineered the GFP gene to function in both Candida albicans. (Reference [18] describes the successful adaptation to Saccharomyces cerevisia as well). In addition to being important organisms for fundamental research in genetics, these yeast are increasingly common pathogens in human illness.
20. Arnone Ml, Bogarad LD, Collazo A, Kirchhamer CV, Cameron RA, Rast JP et at. Green fluorescent protein in the sea urchin: new experimental approaches to transcrip-tional regulatory analysis in embryos and larvae. Development (1997)124:4649-4659. The sea urchin is an important organism for the study of developmental genetics and physiology, making the successful incorporation of GFP an important advance.
21. Wilson LE, Wilkinson N, Martow SA, Possee RD, King LA: Identification of recombinant baculoviruses using green fluorescent protein as a selectable marker. Biotechniques (1997)22:674-681. The authors report the flexible incorporation of a commercially-available gene into an extremely popular insect-compatible expression vector.
22. Leffel SM, Mabon SA, Siewart CN: Applications of green fluorescent protein in plants. Biotechniques (1997) 23:912-916. Describes the adaptation of the GFP gene for use in plants, and provides good overview of the many applications of GFP to the study of plant systems.
23. Collins LA, Torrero MN, Franzblau SG: Green fluorescent protein reporter microplate assay for high-throughput screening of compounds against Mycobacterium tuberculosis. Antimicrobial Agents Chemotherapy(1998) 42:344-347. The first reported use of GFP in a high-throughput-compatible, 36-well microplate fluorescence assay. While the assay was conducted with known compounds, it is clearly ready to be used with unknown substances as well.
24. 2+ based on green fluorescent proteins and calmodulin. Nature (1997) 388:882-887. See reference [25].
25. 2+-dependent changes In the fluorescence emission of an indicator composed of two green fluorescent protein variants linked by a calmodulin-binding sequence - A new class of fluorescent indicators. J Bio/ Chem (1997) 272:13270-13274. Two similar, but independent, reports of the use of calmodulin as a Câ''-dependent switch for modulating FRET between two different-colored GFP mutants. The work in reference [24] incorporates a calmodulin-binding sequence (in addition to calmodulin) between the two GFP domains which improves the properties of the system, and allows the system to function in an intermolecular, as well as intramolecular, fashion.
26. Hanazono Y, Yu JM, Dunbar CE, Emmons RVB: Green fluorescent protein retrovlral vectors: Low titer and high recombination frequency suggest a selective disadvantage. Human Gene Therapy(\$y?) 8:1313-1319. An important recent case study illustrating the down-side of GFP expression. The authors thoroughly characterize a markedly-elevated mutation rate in their GFP-expressing system.
27. Rakhmanova VA, MacDonald RC: A microplate fluorimetric assay for transfection of the β-galactosidase reporter gene. Analytical Biochemistry(1998) 257:234-237. Although fluorescent β-galactosidase reporting systems have been around for a while, this is the first report of their use in a microplate assay amenable to high-throughput screening.
28. Zlokarnik G, Negulescu PA, Knapp TE, Mere L, Burres N, Feng LX et at. Quant it at ion of transcription and clonal selection of single living cells with β-lactamase as reporter. Science (1998) 279:84-88. The authors describe the use of a new membrane-permeant reagent for assaying β-lactamase activity, allowing enzymatic amplification of fluorescence in response to gene expression, as well as two-wavelength detection for improved accuracy. In addition, the use of this assay for a microplate-format assay is reported.
29. Gonzalez JE, Tsien RY: Improved indicators of cell membrane potential that use fluorescence resonance energy transfer. Chemistry & Biology (\y37) 4:269-277. Another landmark paper from one of the leading groups in the field, this system is a significant improvement on earlier work from the same laboratories.
30. Chen C-T, Wagner H, Still WC: Fluorescent, sequence-selective peptide detection by synthetic small molecules. Science (1998) 279:851-853. Based on a series of previous studies of related synthetic receptor systems, the authors report the first use of a fluorescent synthetic receptor to assay combinatorial libraries of substrates.
31. Torrado A, Walkup GK, Impérial B: Exploiting polypeptide motifs for the design of selective Cu (II) ion chemosensor. JAm Chem Soc{1998) 120:609-610. This simple, elegant system already exhibits exceptional selectivities for binding copper in the presence of other metals. Combinatorial libraries of such compounds (hinted at in the closing paragraph of the paper) are sure to bring further exciting results.