Resolving power of dynamic light scattering for protein and polystyrene nanoparticles

References

• Berne BJ, Pecora R. Dynamic light scattering: with applications to chemistry, biology, and physics. Mineola: Dover Publications; 2000
   Google Scholar
• Brown W. Dynamic light scattering: the method and some applications. Oxford: Clarendon Press; 1993
   Google Scholar
• Liao JH, Lee JS, Chiou SH. Distinct roles of alphaA- and alphaB-crystallins under thermal and UV stresses. Biochem Biophys Res Commun 2002;295:854–861
   Google Scholar
• Georgieva D, Schwark D, von BM, et al. Interactions of recombinant prions with compounds of therapeutical significance. Biochem Biophys Res Commun 2006;344:463–470
   PubMed Web of Science ®Google Scholar
• Suzuki S, Wilson-Kubalek EM, Wert D, et al. The oligomeric structure of high molecular weight adiponectin. FEBS Lett 2007;581:809–814
   PubMed Web of Science ®Google Scholar
• Li Y, Lubchenko V, Vekilov PG. The use of dynamic light scattering and Brownian microscopy to characterize protein aggregation. Rev Sci Instrum 2011;82:053106. doi: 10.1063/1.3592581
   PubMed Web of Science ®Google Scholar
• Galantai R, Modos K, Fidy J, et al. Structural basis of the cofactor function of denatured albumin in plasminogen activation by tissue-type plasminogen activator. Biochem Biophys Res Commun 2006;341:736–741
   PubMedGoogle Scholar
• Lind J, Lindahl E, Perálvarez-Marín A, et al. Structural features of proinsulin C-peptide oligomeric and amyloid states. FEBS J 2010;277:3759–3768
   Google Scholar
• Garidel P, Kebbel F. Protein therapeutics and aggregates characterized by photon correlation spectroscopy. Bioprocess Int 2010;8:38–46
   Google Scholar
• Carpenter JF, Randolph TW, Jiskoot W, et al. 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. J Pharm Sci 2010;99:2200–2208
   PubMed Web of Science ®Google Scholar
• Zölls S, Tantipolphan R, Wiggenhorn M, et al. Particles in therapeutic protein formulations, Part 1: overview of analytical methods. J Pharm Sci 2012;101:914–935
   PubMed Web of Science ®Google Scholar
• den Engelsman J, Garidel P, Smulders R, et al. Strategies for the assessment of protein aggregates in pharmaceutical biotech product development. Pharm Res 2011;28:920–933
   PubMed Web of Science ®Google Scholar
• Narhi LO, Schmit J, Bechtold-Peters K, Sharma D. Classification of protein aggregates. J Pharm Sci 2012;101:493–498
   PubMed Web of Science ®Google Scholar
• Rosenberg AS. Effects of protein aggregates: an immunologic perspective. AAPS J 2006;8:E501–E507
   PubMed Web of Science ®Google Scholar
• Carpenter JF, Randolph TW, Jiskoot W, et al. Overlooking subvisible particles in therapeutic protein products: gaps that may compromise product quality. J Pharm Sci 2009;98:1201–1205
   PubMed Web of Science ®Google Scholar
• Kaszuba M, Connah MT, Neil-Watson FK, Nobbmann U. Resolving concentrated particle size mixtures using dynamic light scattering. Part Part Syst Charact 2007;24:159–162
   Web of Science ®Google Scholar
• Filipe V, Hawe A, Jiskoot W. Critical evaluation of nanoparticle tracking analysis (NTA) by NanoSight for the measurement of nanoparticles and protein aggregates. Pharm Res 2010;27:796–810
   PubMed Web of Science ®Google Scholar
• Jamting AK, Cullen J, Coleman VA, et al. Systematic study of bimodal suspensions of latex nanoparticles using dynamic light scattering. Adv Powder Technol 2011;22:290–293
   Google Scholar
• Hanus LH, Ploehn HJ. Conversion of intensity-averaged photon correlation spectroscopy measurements to number-averaged particle size distributions. 1. Theoretical development. Langmuir 1999;15:3091–3100
   Google Scholar
• Arakawa T, Philo JS, Ejima D, et al. Aggregation analysis of therapeutic proteins, Part 2. BioProcess Int 2007;5:36–47
   Google Scholar
• Finsy R, Deriemaeker L, De Jaeger N, et al. Particle sizing by photon correlation spectroscopy. Part IV; resolution of bimodals and comparison with other particle sizing methods. Part Part Syst Charact 1993;10:118–128
   Web of Science ®Google Scholar
• Rasteiro MG, Lemos CC, Vasquez A. Nanoparticle characterization by PCS: the analysis of bimodal distributions. Part Sci Technol 2008;26:413–437
   Web of Science ®Google Scholar
• International Organization for Standardization (ISO). ISO13321 IS. 1996
   Google Scholar
• Bergemann K, Eckermann C, Garidel P, et al. Production and downstream processing. In: Dübel S, ed. Handbook of therapeutic antibodies. Weinheim: John Wiley & Sons; 2007:199–238
   Google Scholar
• Xu R. Particle characterization: light scattering methods. Dordrecht: Kluwer Academic; 2000
   Google Scholar
• den Engelsman J, Kebbel F, Garidel P. Laser light scattering-based techniques used for the characterisation of protein therapeutics. In: Mahler HC, Jiskoot W, ed. Analysis of aggregates and particles in protein pharmaceuticals. Chapter 3. New Jersey: John Wiley & Sons; 2012:37–60
   Google Scholar
• Ripple DC, Wayment JR, Carrier MJ. Standards for the optical detection of protein particles. Am Pharma Rev 2011;14:90–96
   Google Scholar
• Garidel P, Herre A, Kliche W. Microscopic methods for particle characterisation in protein pharmaceuticals. In: Mahler HC, Jiskoot W, eds. Analysis of aggregates and particles in protein pharmaceuticals. Chapter 12. New Jersey: John Wiley & Sons; 2012:269–302
   Google Scholar
• Foladori P, Quaranta A, Ziglio G. Use of silica microspheres having refractive index similar to bacteria for conversion of flow cytometric forward light scatter into biovolume. Water Res 2008;42:3757–3766
   Google Scholar
• Chandler WL, Yeung W, Tait JF. A new microparticle size calibration standard for use in measuring smaller microparticles using a new flow cytometer. J Thromb Haemost 2011;9:1216–1224
   PubMed Web of Science ®Google Scholar
• Barnard JG, Singh S, Randolph TW, Carpenter JF. Subvisible particle counting provides a sensitive method of detecting and quantifying aggregation of monoclonal antibody caused by freeze-thawing: insights into the roles of particles in the protein aggregation pathway. J Pharm Sci 2011;100:492–503
   PubMed Web of Science ®Google Scholar
• Brummitt RK, Nesta DP, Chang L, et al. Nonnative aggregation of an IgG1 antibody in acidic conditions: part 1. Unfolding, colloidal interactions, and formation of high-molecular-weight aggregates. J Pharm Sci 2011;100:2087–2103
   PubMed Web of Science ®Google Scholar