BIAcore for macromolecular interaction

Current Opinion in Biotechnology

Volumn 9, Issue 1, 1998, Pages 97-101

  Fivash, Matthew ^a   Towler, Eric M ^a   Fisher, Robert J ^a  

^a SAIC FREDERICK INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOTECHNOLOGY; MACROMOLECULE; MASS SPECTROMETRY; MOLECULAR INTERACTION; PRIORITY JOURNAL; REVIEW; SPECTROSCOPY; TECHNIQUE;

EID: 0031933809     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(98)80091-8     Document Type: Article

References (34)

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2. Schier R, Bye J, Apell G, McCall A, Adams GP, Malmqvist M, Weiner LM, Marks JD. Isolation of high-affinity monomeric human anti-c-erbB-2 single chain Fv using affinity-driven selection. of special interest J Mol Biol. 255:1996;28-43 The concentration of binding phage was determined by measuring the rate of binding to c-erbB-2 extra-cellular domain under transport-limiting conditions in order to determine the amount of antigen to be used in the next round of selection. It seems that whereas the BIAcore was used for routine measurements it was not used in the actual selection of high affinity phage expressing scFv.
3. Medina MB. Hygromycin B antibody production and characterization by a surface plasmon resonance biosensor. J Agricultural Food Chem. 45:1997;389-394.
4. Oddie GW, Gruen LC, Odgers GA, King LG, Kortt AA. Identification and minimization of nonideal binding effects in BIAcore analysis: ferritin/anti-ferritin Fab' interaction as a model system. of special interest Anal Biochem. 244:1997;301-311 An example of how to manipulate binding conditions with the surface density of the ligand and flow rate.
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6. Autiero M, Gaubin M, Mani J-C, Castejon C, Martin M, El Marhomy S, Guardiola J, Piatier-Tonneau D. Surface plasmon resonance analysis of gp17, a natural CD4 ligand from human seminal plasma inhibiting human immunodeficiency virus type-1 gp120-mediated syncytium formation. Eur J Biochem. 245:1997;208-213.
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12. ds determined by Tm, calorimetry and BIAcore was noted, the discrepancy was three orders of magnitude.
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14. Lin Z, Eisenstein E. Nucleotide binding-promoted conformational changes release a non-native polypeptide from the Escherichia coli chaperonin GroEL. of outstanding interest Proc Natl Acad Sci USA. 93:1996;1977-1981 The dissociation of GroEL from surface-bound subtilisin demonstrated two sigmoidal transitions in the presence of AMP-PNP, suggesting that substrate dissociation from GroEL is limited by a concerted conformational change that follows nucleotide binding.
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17. Krone JR, Nelson RW, Dogruel D, Williams P, Granzow R. BIA/MS: interfacing biomolecular interaction analysis with mass spectrometry. of outstanding interest Anal Biochem. 244:1997;124-132 A novel approach to identify the surface bound (BIAcore CM5 chip) material directly. This type of analysis will grow explosively in the next few years. This way of examining the surface will allow direct estimates about the uniformity of the surface bound analytes.
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19. Lackmann M, Bucci T, Mann RJ, Kravets LA, Viney E, Smith F, Moritz RL, Carter W, Simpson RJ, Nicola NA, et al. Purification of a ligand for the EPH-like receptor HEK using a biosensor-based affinity detection approach. Proc Natl Acad Sci USA. 93:1996;2523-2527.
20. Kuziemko GM, Stroh M, Stevens RC. Cholera toxin binding affinity and specificity for gangliosides determined by surface plasmon resonance. of outstanding interest Biochemistry. 35:1996;6375-6384 The gold chip was removed from a CM5 sensor chip by soaking in ethanol and the gold surface was cleaned and reconditioned in a PDC-236 plasma cleaner. The surface hydrophobic surface was remade by soaking the cleaned chip in 0.1% octadecylmercaptan. The gangliosides were added directly to the surface to mimic a cell membrane. The picomolar equilibrium constants are among the lowest measured by surface plasmon resonance spectroscopy.
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24. Fisher RJ, Fivash M, Casas-Finet J, Bladen S, McNitt KL. Real-time BIAcore measurements of Escherichia coli single-stranded DNA binding (SSB) protein to polydeoxythymidylic acid reveal single-state kinetics with steric cooperativity. Methods: A Companion to Methods in Enzymology. 6:1994;121-133.
25. Fisher RJ, Fivash M. Surface plasmon resonance based methods for measuring the kinetics and binding affinities of biomolecular interactions. Curr Opin Biotechnol. 5:1994;389-395.
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27. O'Connor-McCourt M: The analysis of surface plasmon resonance-based biosensor data using numerical integration: the epidermal growth factor receptor-ligand interaction as an example. In Quantitative Analysis of Biospecific Interactions. Edited by Lundquist A, Greijer E. In press.
28. Myszka DG. Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors. of outstanding interest Curr Opin Biotechnol. 8:1997;50-57 This review of kinetic analysis of BIAcore data shows the usefulness of global modeling. Material transport effects are included in the program Myszka provides. Material transport effects are a part of nearly all BIAcore instrument data, any useful estimate of binding constants must acknowledge this fact. We note that non-specific binding is generally a convolution effect, and can not be removed through simple subtraction of a reference surface. Instrument noise, such as injection refractive index shift, is an example of additive noise, and may be subtracted from a binding signal.
29. BIACORE. BIAevaluation 3.0. 1997.
30. Calculation of molarity in the sensor chip CM5 matrix. BIAifo FAX 1001. 1991.
31. Christensen LLH. Theoretical analysis of protein concentration determination using biosensor technology under conditions of partial transport limitation. of outstanding interest of special interest Anal Biochem. 249:1997;153-164 This paper shows that the two-compartment model, first shown by Fisher and Fivash in 1994 (25), holds for the initial slopes of a sensogram set. Christensen arrives to the initial slopes equation through considering a continuous convective-diffusive system. We note that the same equation is immediately available through the two-compartment model. The techniques in this paper have already found practical use in BIAcore experiments (see also Richalet-Sécordel et al. 1997 [32]).
32. Richalet-Sécordel PM, Rauffer-Bruyère N, Christensen LLH, Ofenloch-Haehnle B, Seidel C, Van Reqgenmortel MHV. Concentration measurement of unpurified proteins using biosensor technology under conditions of part mass transport limitation. of outstanding interest Anal Biochem. 249:1997;165-173 This use of initial slope analysis, by varying the flow rate, shows good prospects as a standard technique. We recommend surface density titers as well as flow rate titers in a more complete analysis of concentration.
33. Werner MH, Clore GM, Fisher CL, Fisher RJ, Trinh L, Shiloach J, Gronenborn AM. Correction of the NMR structure of the ETS1/DNA complex. J Biomolec NMR. 1997;. in press.
34. Fisher RJ, Fivash M, Casas-Finet J, Erickson JW, Kondoh A, Bladen SV, Fisher C, Watson DK, Papas T. Real-time DNA binding measurements of the ETS1 recombinant oncoproteins reveal significant kinetic differences between the p42 and p51 isoforms. Protein Sci. 3:1994;257-266.