User menu

High-throughput assessment of antigen conformational stability by ultraviolet absorption spectroscopy and its application to excipient screening

Bibliographic reference Dasnoy, Sébastien ; Le Bras, Vivien ; Préat, Véronique ; Lemoine, Dominique. High-throughput assessment of antigen conformational stability by ultraviolet absorption spectroscopy and its application to excipient screening. In: Biotechnology and Bioengineering, Vol. 109, no.2, p. 502-516 (2012)
Permanent URL http://hdl.handle.net/2078.1/120122
  1. Arakawa T., Timasheff S.N., The stabilization of proteins by osmolytes, 10.1016/s0006-3495(85)83932-1
  2. Arakawa Tsutomu, Ejima Daisuke, Tsumoto Kouhei, Obeyama Noriyuki, Tanaka Yoshikazu, Kita Yoshiko, Timasheff Serge N., Suppression of protein interactions by arginine: A proposed mechanism of the arginine effects, 10.1016/j.bpc.2006.12.007
  3. Aucamp Jean P., Cosme Ana M., Lye Gary J., Dalby Paul A., High-throughput measurement of protein stability in microtiter plates, 10.1002/bit.20397
  4. Ausar Salvador F., Espina Marianela, Brock Julie, Thyagarayapuran Nagarajan, Repetto Robert, Khandke Lakshmi, Middaugh C. Russell, High-throughput screening of stabilizers for Respiratory Syncytial Virus: Identification of stabilizers and their effects on the conformational thermostability of viral particles, 10.4161/hv.3.3.4149
  5. Capelle Martinus A. H., Gurny Robert, Arvinte Tudor, A High Throughput Protein Formulation Platform: Case Study of Salmon Calcitonin, 10.1007/s11095-008-9662-8
  6. Dasnoy Sébastien, Dezutter Nancy, Lemoine Dominique, Le Bras Vivien, Préat Véronique, High-Throughput Screening of Excipients Intended to Prevent Antigen Aggregation at Air-Liquid Interface, 10.1007/s11095-011-0393-x
  7. Eftink Maurice R, Use of fluorescence spectroscopy as thermodynamics tool, Methods in Enzymology (2000) ISBN:9780121822248 p.459-473, 10.1016/s0076-6879(00)23378-8
  8. He Feng, Joshi Sangeeta B., Moore David D., Shinogle Heather E., Ohtake Satoshi, Lechuga-Ballesteros David, Martin Russell A., Truong-Le Vu L., Middaugh C. Russell, Using spectroscopic and microscopic methods to probe the structural stability of human adenovirus type 4, 10.4161/hv.6.2.10254
  9. Hermeling Suzanne, Crommelin Daan J. A., Schellekens Huub, Jiskoot Wim, Structure-Immunogenicity Relationships of Therapeutic Proteins, 10.1023/b:pham.0000029275.41323.a6
  10. Kissmann Julian, Ausar Salvador F., Foubert Thomas R., Brock Julie, Switzer Mary H., Detzi Edward J., Vedvick Thomas S., Middaugh C.Russell, Physical Stabilization of Norwalk Virus‐Like Particles**The views, opinions and/or findings contained in this report are those of the author(s) and should not be construed as an official Department of the Army position, policy or decision unless so designated by other documentation., 10.1002/jps.21315
  11. Kissmann Julian, Ausar Salvador F., Rudolph Angela, Braun Chad, Cape Stephen P., Sievers Robert E., Federspiel Mark J., Joshi Sangeeta B., Middaugh C. Russell, Stabilization of measles virus for vaccine formulation, 10.4161/hv.4.5.5863
  12. Kueltzo Lisa A., Normand Nadia, O'Hare Peter, Middaugh C. Russell, Conformational Lability of Herpesvirus Protein VP22, 10.1074/jbc.m002476200
  13. Lakowicz, Principles of fluorescence spectroscopy, 725 (2004)
  14. Leach S. J., Scheraga H. A., Effect of Light Scattering on Ultraviolet Difference Spectra1, 10.1021/ja01503a008
  15. Liu Pei-Fen, Avramova Larisa V., Park Chiwook, Revisiting absorbance at 230nm as a protein unfolding probe, 10.1016/j.ab.2009.03.028
  16. Mach Henryk, Middaugh C. Russell, Ultraviolet Spectroscopy as a Tool in Therapeutic Protein Development, 10.1002/jps.22385
  17. Mahendrarajah Kumaran, Dalby Paul A., Wilkinson Barrie, Jackson Sophie E., Main Ewan R.G., A high-throughput fluorescence chemical denaturation assay as a general screen for protein–ligand binding, 10.1016/j.ab.2010.12.001
  18. Malo Nathalie, Hanley James A., Carlile Graeme, Liu Jing, Pelletier Jerry, Thomas David, Nadon Robert, Experimental Design and Statistical Methods for Improved Hit Detection in High-Throughput Screening, 10.1177/1087057110377497
  19. McGown Evelyn L., Hafeman Dean G., Multichannel Pipettor Performance Verified by Measuring Pathlength of Reagent Dispensed into a Microplate, 10.1006/abio.1998.2621
  20. Pace, Protein structure: A practical approach, 299 (1997)
  21. Park Man Ki, Park Jeong Hill, Cho Jung Hwan, Qualitative analysis by derivative spectrophotometry (II) : Computer-assisted spectral analysis using derivative spectra and root mean of squares of differences, 10.1007/bf02911062
  22. Peek Laura J., Brey Robert N., Middaugh C.Russell, A Rapid, Three-Step Process for the Preformulation of aRecombinant Ricin Toxin A-Chain Vaccine, 10.1002/jps.20675
  23. Prestrelski S.J., Arakawa T., Carpenter J.F., Separation of Freezing- and Drying-Induced Denaturation of Lyophilized Proteins Using Stress-Specific Stabilization, 10.1006/abbi.1993.1310
  24. Ragone Raffaele, Colonna Giovanni, Balestrieri Ciro, Servillo Luigi, Irace Gaetano, Determination of tyrosine exposure in proteins by second-derivative spectroscopy, 10.1021/bi00303a044
  25. Savitzky Abraham., Golay M. J. E., Smoothing and Differentiation of Data by Simplified Least Squares Procedures., 10.1021/ac60214a047
  26. Sellers, Methods Mol Biol, 308, 243 (2005)
  27. Senisterra Guillermo A., Finerty, Jr Patrick J., High throughput methods of assessing protein stability and aggregation, 10.1039/b814377c
  28. Senisterra Guillermo A., Soo Hong Bum, Park Hee-Won, Vedadi Masoud, Application of High-Throughput Isothermal Denaturation to Assess Protein Stability and Screen for Ligands, 10.1177/1087057108317825
  29. Shire Steven J, Formulation and manufacturability of biologics, 10.1016/j.copbio.2009.10.006
  30. Tavornvipas Sumitra, Hirayama Fumitoshi, Takeda Seiko, Arima Hidetoshi, Uekama Kaneto, Effects of Cyclodextrins on Chemically and Thermally Induced Unfolding and Aggregation of Lysozyme and Basic Fibroblast Growth Factor, 10.1002/jps.20715
  31. Thirumangalathu Renuka, Krishnan Sampathkumar, Bondarenko Pavel, Speed-Ricci Margaret, Randolph Theodore W., Carpenter John F., Brems David N., Oxidation of Methionine Residues in Recombinant Human Interleukin-1 Receptor Antagonist:  Implications of Conformational Stability on Protein Oxidation Kinetics†, 10.1021/bi700321g
  32. Thirumangalathu Renuka, Krishnan Sampathkumar, Ricci Margaret Speed, Brems David N., Randolph Theodore W., Carpenter John F., Silicone Oil- and Agitation-Induced Aggregation of a Monoclonal Antibody in Aqueous Solution, 10.1002/jps.21719
  33. Thomson, J Biol Chem, 264, 11614 (1989)
  34. Tukey, Exploratory data analysis, 688 (1977)
  35. Vessely Christina, Estey Tia, Randolph Theodore W., Henderson Ian, Cooper Julianne, Nayar Rajiv, Braun Latoya Jones, Carpenter John F., Stability of a Trivalent Recombinant Protein Vaccine Formulation Against Botulinum Neurotoxin During Storage in Aqueous Solution, 10.1002/jps.21498
  36. Wang Wei, Protein aggregation and its inhibition in biopharmaceutics, 10.1016/j.ijpharm.2004.11.014
  37. Zhang J.-H., A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays, 10.1177/108705719900400206
  38. Zhao Hui, Graf Olivier, Milovic Nebojsa, Luan Xiaosong, Bluemel Markus, Smolny Markus, Forrer Kurt, Formulation Development of Antibodies Using Robotic System and High-Throughput Laboratory (HTL), 10.1002/jps.22008