2013
DOI: 10.1002/jps.23746
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Utilizing Dynamic Light Scattering as a Process Analytical Technology for Protein Folding and Aggregation Monitoring in Vaccine Manufacturing

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Cited by 66 publications
(50 citation statements)
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“…4(a) and (b). The vast difference in the values can be attributed to hydrodynamic diameter of NiO NPs which include solvation layers [50]. Since the scattering intensity is directly proportional to the sixth power of the particle radius, this technique is extremely sensitive towards the presence of small aggregates and dense materials like metal oxides resulting in overestimation of particle size and conflicting data [51,52].…”
Section: Structure Morphology and Other Physical Propertiesmentioning
confidence: 99%
“…4(a) and (b). The vast difference in the values can be attributed to hydrodynamic diameter of NiO NPs which include solvation layers [50]. Since the scattering intensity is directly proportional to the sixth power of the particle radius, this technique is extremely sensitive towards the presence of small aggregates and dense materials like metal oxides resulting in overestimation of particle size and conflicting data [51,52].…”
Section: Structure Morphology and Other Physical Propertiesmentioning
confidence: 99%
“…However, unfolding does lead to changes in DLS, which is sensitive to changes in scatterer size. We are aware of only one publication reporting the use of DLS to monitor chemical denaturation, and the work presented is only preliminary [20]. The technique is promising and deserves further development.…”
Section: Applicationsmentioning
confidence: 99%
“…Yu et al (2013) used dynamic light scattering ( DLS ) to monitor the refolding process of a protein-based vaccine candidate. As this method has no need for an intrinsic or extrinsic fluorophore, it is not restricted to proteins with distinct properties.…”
Section: Monitoring Toolsmentioning
confidence: 99%
“…As DLS measurements are non-intrusive, aggregation or dissociation caused by the assay is greatly decreased. Concerning the precision of the rH values (particle size information) Yu et al (2013) reported that a difference of 1.5 nm is reliable. Protein concentrations of 0.05–0.1 g/l were reported to give the best results (Bhattacharjee 2016).…”
Section: Monitoring Toolsmentioning
confidence: 99%
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