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High-throughput screening of excipients intended to prevent antigen aggregation at air-liquid interface.

Bibliographic reference 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.. In: Pharmaceutical Research, Vol. 28, no. 7, p. 1591-605 (2011)
Permanent URL http://hdl.handle.net/2078.1/77773
  1. Rathore N., Rajan R.S., Current Perspectives on Stability of Protein Drug Products during Formulation, Fill and Finish Operations, 10.1021/bp070462h
  2. Wang Wei, Protein aggregation and its inhibition in biopharmaceutics, 10.1016/j.ijpharm.2004.11.014
  3. Hermeling Suzanne, Crommelin Daan J. A., Schellekens Huub, Jiskoot Wim, Structure-Immunogenicity Relationships of Therapeutic Proteins, 10.1023/b:pham.0000029275.41323.a6
  4. Hlady Vladimir, Buijs Jos, Jennissen Herbert P., [26] Methods for studying protein adsorption, Methods in Enzymology (1999) ISBN:9780121822101 p.402-429, 10.1016/s0076-6879(99)09028-x
  5. Sluzky V., Tamada J. A., Klibanov A. M., Langer R., Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces., 10.1073/pnas.88.21.9377
  6. Katakam M, Banga AK. Aggregation of insulin and its prevention by carbohydrate excipients. PDA J Pharm Sci Technol. 1995;49(4):160–5.
  7. Bringer J., Heldt A., Grodsky G. M., Prevention of insulin aggregation by dicarboxylic amino acids during prolonged infusion, 10.2337/diabetes.30.1.83
  8. Soenderkaer S., van de Weert M., Lindgaard Hansen L., Flink J., Frokjaer S., Evaluation of statistical design/modeling for prediction of the effect of amino acids on agitation-induced aggregation of human growth hormone and human insulin, 10.1016/s1773-2247(05)50083-2
  9. Quinn R., Andrade J.D., Minimizing the Aggregation of Neutral Insulin Solutions, 10.1002/jps.2600721227
  10. Charman Susan A., Mason Kaye L., Charman William N., 10.1023/a:1018994102218
  11. Maa Yuh-Fun, Hsu Chung C., Protein denaturation by combined effect of shear and air-liquid interface, 10.1002/(sici)1097-0290(19970620)54:6<503::aid-bit1>3.0.co;2-n
  12. Katakam Manohar, Banga Ajay K., Use of Poloxamer Polymers to Stabilize Recombinant Human Growth Hormone Against Various Processing Stresses, 10.3109/10837459709022619
  13. Katakam Manohar, Bell Leonard N., Banga Ajay K., Effect of Surfactants on the Physical Stability of Recombinant Human Growth Hormone, 10.1002/jps.2600840609
  14. Bam Narendra B., Cleland Jeffrey L., Yang Janet, Manning Mark C., Carpenter John F., Kelley Robert F., Randolph║ Theodore W., Tween protects recombinant human growth hormone against agitation-induced damage via hydrophobic interactions, 10.1021/js980175v
  15. Hagenlocher M, Pearlman R. Use of a substituted cyclodextrin for stabilization of solutions of recombinant human growth hormone. Pharm Res. 1989;6:S30.
  16. Chou Danny K., Krishnamurthy Rajesh, Randolph Theodore W., Carpenter John F., Manning Mark Cornell, Effects of Tween 20® and Tween 80® on the Stability of Albutropin During Agitation, 10.1002/jps.20365
  17. Mahler Hanns-Christian, Müller Robert, Frieβ Wolfgang, Delille Aurelie, Matheus Susanne, Induction and analysis of aggregates in a liquid IgG1-antibody formulation, 10.1016/j.ejpb.2004.12.004
  18. Kiese Sylvia, Papppenberger Astrid, Friess Wolfgang, Mahler Hanns-Christian, Shaken, Not Stirred: Mechanical Stress Testing of an IgG1 Antibody, 10.1002/jps.21328
  19. Serno Tim, Carpenter John F., Randolph Theodore W., Winter Gerhard, Inhibition of Agitation‐Induced Aggregation of an IgG‐Antibody by Hydroxypropyl‐β‐Cyclodextrin, 10.1002/jps.21931
  20. 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
  21. Joshi Omkar, Chu Liping, McGuire Joseph, Wang D.Q., Adsorption and function of recombinant Factor VIII at the air–water interface in the presence of Tween 80, 10.1002/jps.21569
  22. Krielgaard Lotte, Jones Latoya S., Randolph Theodore W., Frokjaer Sven, Flink James M., Manning Mark C., Carpenter John F., Effect of tween 20 on freeze-thawing- and agitation-induced aggregation of recombinant human factor XIII, 10.1021/js980126i
  23. Wang Wei, Wang Y. John, Wang D.Q., Dual effects of Tween 80 on protein stability, 10.1016/j.ijpharm.2007.06.042
  24. Banga A., Mitra R., Minimization of Shaking-induced Formation of Insoluble Aggregates of Insulin by Cyclodextrins, 10.3109/10611869308996093
  25. 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
  26. 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
  27. Ausar Salvador F., Chan Judy, Hoque Warda, James Olive, Jayasundara Kavisha, Harper Kevin, Application of Extrinsic Fluorescence Spectroscopy for the High Throughput Formulation Screening of Aluminum-Adjuvanted Vaccines, 10.1002/jps.22282
  28. Kyte Jack, Doolittle Russell F., A simple method for displaying the hydropathic character of a protein, 10.1016/0022-2836(82)90515-0
  29. Lakowicz JR. Principles of fluorescence spectroscopy. New York: Springer; 2004.
  30. McGown Evelyn L., Hafeman Dean G., Multichannel Pipettor Performance Verified by Measuring Pathlength of Reagent Dispensed into a Microplate, 10.1006/abio.1998.2621
  31. Goormaghtigh Erik, Ruysschaert Jean-Marie, Raussens Vincent, Evaluation of the Information Content in Infrared Spectra for Protein Secondary Structure Determination, 10.1529/biophysj.105.072017
  32. Kendrick Brent S., Dong Aichun, Dean Allison S., Manning Mark C., Carpenter John F., Quantitation of the Area of Overlap between Second-Derivative Amide I Infrared Spectra To Determine the Structural Similarity of a Protein in Different States, 10.1021/js950332f
  33. Oehlert GW. A first course in design and analysis of experiments. New York: W.H. Freeman & Co; 2000.
  34. Zhang J.-H., A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays, 10.1177/108705719900400206
  35. Sackett Dan L., Wolff J., Nile red as a polarity-sensitive fluorescent probe of hydrophobic protein surfaces, 10.1016/0003-2697(87)90157-6
  36. Sutter Marc, Oliveira Sabrina, Sanders Niek N., Lucas Bart, van Hoek Arie, Hink Mark A., Visser Antonie J. W. G., De Smedt Stefaan C., Hennink Wim E., Jiskoot Wim, Sensitive Spectroscopic Detection of Large and Denatured Protein Aggregates in Solution by Use of the Fluorescent Dye Nile Red, 10.1007/s10895-007-0156-6
  37. Byler D. Michael, Susi Heino, Examination of the secondary structure of proteins by deconvolved FTIR spectra, 10.1002/bip.360250307
  38. Dong Aichun, Huang Ping, Caughey Winslow S., Protein secondary structures in water from second-derivative amide I infrared spectra, 10.1021/bi00465a022
  39. Pain RH. Determining the fluorescence spectrum of a protein. Curr Protoc Protein Sci. 2004;S38:7.7.1–7.7.20.
  40. Carpenter John F., Randolph Theodore W., Jiskoot Wim, Crommelin Daan J.A., Middaugh C.Russell, Winter Gerhard, Potential inaccurate quantitation and sizing of protein aggregates by size exclusion chromatography: Essential need to use orthogonal methods to assure the quality of therapeutic protein products, 10.1002/jps.21989
  41. Jorgensen Lene, Hostrup Susanne, Moeller Eva Horn, Grohganz Holger, Recent trends in stabilising peptides and proteins in pharmaceutical formulation – considerations in the choice of excipients, 10.1517/17425240903199143
  42. Samra Hardeep S., He Feng, Bhambhani Akhilesh, Pipkin J.D., Zimmerer Roz, Joshi Sangeeta B., Russell Middaugh C., The Effects of Substituted Cyclodextrins on the Colloidal and Conformational Stability of Selected Proteins, 10.1002/jps.22053
  43. Saski Witold, Shah S.G., Availability of Drugs in the Presence of Surface-Active Agents I: Critical Micelle Concentrations of Some Oxyethylene Oxypropylene Polymers, 10.1002/jps.2600540117
  44. Rassing J., Attwood D., Ultrasonic velocity and light-scattering studies on the polyoxyethylene—polyoxypropylene copolymer Pluronic F127 in aqueous solution, 10.1016/0378-5173(82)90141-7