Dynamic light scattering as a relative tool for assessing the molecular integrity and stability of monoclonal antibodies

Nobbmann, Ulf; Connah, Malcolm T.; Fish, Brendan; Varley, Paul; Gee, Chris; Mulot, Sandrine; Chen, Juntao; Zhou, Liang; Lu, Youming; Sheng, Fei; Yi, Junming; Harding, Stephen E.

doi:10.1080/02648725.2007.10648095

Cited by 177 publications

(113 citation statements)

References 12 publications

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“…2). For instance, the 0.8 mM gold chloride solution forms monodisperse GNPs (PDI <0.1) [25,26] for a range of Ct/Au ratios from 4:1 to 13:1, whereas only a very narrow range of Ct/Au ratios (5:1 to 6:1) produces monodisperse GNPs when starting with 2.0 mM gold chloride solutions (Table 1). From these data, we can conclude that, depending on the starting concentration of gold salt, a wider or narrower range of Ct/Au ratios allows for the formation of monodisperse GNPs.…”

Section: Resultsmentioning

confidence: 99%

“…The size of the formed GNPs presents a minimum at Ct/ Au ratios around 4:1-5:1 and saturates at high ratios (>10:1). However, gold salt solutions over 0.8 mM lead to the formation of monodisperse GNPs (PDI<0.1) [25,26,28] only for a certain range of Ct/Au ratios, which becomes narrower as the concentration of gold(III) increases. Also, the size of these GNPs presents a minimum at specific Ct/Au ratios, but increases unboundedly at high ratios, accompanied by an increase of the corresponding PDI.…”

Section: Resultsmentioning

confidence: 99%

“…Consequently, for gold(III) solutions below 0.8 mM, the largest monodisperse GNPs (PDI<0.1) [25,26,28] have a polydispersity curve that reaches a plateau at high Ct/Au ratios. For instance, the largest HD that can be obtained from 0.3 and 0.6 mM gold(III) solutions in a monodisperse manner are about 27 and 18 nm, respectively.…”

Section: Modelingmentioning

confidence: 99%

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Effect of high gold salt concentrations on the size and polydispersity of gold nanoparticles prepared by an extended Turkevich–Frens method

et al. 2012

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The Turkevich-Frens synthesis starting conditions are expanded, ranging the gold salt concentrations up to 2 mM and citrate/gold(III) molar ratios up to 18:1. For each concentration of the initial gold salt solution, the citrate/gold(III) molar ratios are systematically varied from 2:1 to 18:1 and both the size and size distribution of the resulting gold nanoparticles are compared. This study reveals a different nanoparticle size evolution for gold salt solutions ranging below 0.8 mM compared to the case of gold salt solutions above 0.8 mM. In the case of [Au 3+ ]<0.8 mM, both the size and size distribution vary substantially with the citrate/gold(III) ratio, both displaying plateaux that evolve inversely to [Au 3+ ] at larger ratios. Conversely, for [Au 3+ ]≥0.8 mM, the size and size distribution of the synthesized gold nanoparticles continuously rise as the citrate/gold(III) ratio is increased. A starting gold salt concentration of 0.6 mM leads to the formation of the most monodisperse gold nanoparticles (polydispersity index< 0.1) for a wide range of citrate/gold(III) molar ratios (from 4:1 to 18:1). Via a model for the formation of gold nanoparticles by the citrate method, the experimental trends in size could be qualitatively predicted: the simulations showed that the destabilizing effect of increased electrolyte concentration at high initial [Au 3+ ] is compensated by a slight increase in zeta potential of gold nanoparticles to produce concentrated dispersion of gold nanoparticles of small sizes.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Effect of high gold salt concentrations on the size and polydispersity of gold nanoparticles prepared by an extended Turkevich–Frens method

et al. 2012

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“…Most of the proteins are seen tightly dispersed around a hydrodynamic diameter of 4 nm and some aggregation is observed (larger aggregates near one micron in size), consistent with work seen in the literature. 50 To compare, the dotted line shows the size distribution of a solution of the same BSA stored at room temperature for one week at 1 mg/mL. Again, a large fraction of the BSA exists as monomers with some larger aggregates observed.…”

Section: Initial Model System Results Showing Hindered Protein Aggregmentioning

confidence: 99%

Stabilizing Biomacromolecules in Nontoxic Nano-Structured Materials

Domach

Walker

2010

JALA: Journal of the Association for Laboratory Automation

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Increases in the use of protein-based pharmaceuticals require the development of cost-effective methods of storage and transport of sensitive biomolecules. In this article, we review the general problems of protein stabilization, aspects specific to antibodies, and a proposed method for protecting proteins based on nanostructured hydrogels. This review is not intended to be comprehensive, but instead to provide the reader with specific examples that capture some of the key challenges and opportunities of the field.

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“…Solution molecular mass and aggregation state was assessed by dynamic light scattering, DLS, using a Malvern Intruments Zetasizer Nano S. For these experiments, proteins were prepared at 1 to 3 mg/ml in PBS, and dust removed by centrifugation at 13000 rpm in a microcentrifuge for 20 minutes immediately before each experiment. Scattered intensity profiles at 630 nm were acquired for 10 second periods and converted to correlograms of the autocorrelation signal as a function of time using the DTS Nano software provided by the manufacturer [20]. These correlograms were then transformed to size distributions using the same software, and both the raw distribution as a function of intensity, as well as the mass weighted distribution, is reported.…”

Section: Cloning and Protein Expressionmentioning

confidence: 99%

Stability of dystrophin STR fragments in relation to junction helicity

Mirza

Menhart

2008

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Dystrophin is a rod shaped protein consisting of amino-and carboxy-terminal binding domains linked by a large central rod composed of 24 homologous copies of the STR motif and 4 nonhomologous regions termed hinges. These hinges are proposed to confer local flexibility; conversely, the tacit implication is that the STR regions away from the hinges are comparatively rigid. This, and the repeating nature of this rod, has contributed to the view that the STR region of the rod is uniform and monolithic. However, we have produced various 2 STR fragments, chosen to have high and low α-helix content at their junctions with each other, and show that they exhibit markedly different stabilities. In contrast to a related protein, spectrin, these differences are not correlated with the calculated helicity, but appear to be an intrinsic property of the motifs themselves. A full understanding of how these properties vary along the length of the rod has implications for the engineering of these rods regions in exon-skipping and mini-dystrophin therapies.

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Dynamic light scattering as a relative tool for assessing the molecular integrity and stability of monoclonal antibodies

Abstract: Harding (2007) Dynamic light scattering as a relative tool for assessing the molecular integrity and stability of monoclonal antibodies, Biotechnology and Genetic Engineering Reviews, 24:1, 117-128,

Cited by 177 publications

References 12 publications

Effect of high gold salt concentrations on the size and polydispersity of gold nanoparticles prepared by an extended Turkevich–Frens method

Effect of high gold salt concentrations on the size and polydispersity of gold nanoparticles prepared by an extended Turkevich–Frens method

Stabilizing Biomacromolecules in Nontoxic Nano-Structured Materials

Stability of dystrophin STR fragments in relation to junction helicity

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