Nonionic Surfactant Brij 35 in Water and in Various Simple Alcohols:  Structural Investigations by Small-Angle X-ray Scattering and Dynamic Light Scattering

2004 ◽  
Vol 108 (22) ◽  
pp. 7021-7032 ◽  
Author(s):  
Matija Tomšič ◽  
Marija Bešter-Rogač ◽  
Andrej Jamnik ◽  
Werner Kunz ◽  
Didier Touraud ◽  
...  
Keyword(s):  
Light Scattering ◽  
Dynamic Light Scattering ◽  
Nonionic Surfactant ◽  
Small Angle ◽  
Structural Investigations ◽  
X Ray ◽  
X Ray Scattering ◽  
Brij 35 ◽  
Ray Scattering

scholarly journals Use of dynamic light scattering and small-angle X-ray scattering to characterize new surfactants in solution conditions for membrane-protein crystallization

2015 ◽  
Vol 71 (7) ◽  
pp. 838-846 ◽  
Author(s):  
Mohamed Dahani ◽  
Laurie-Anne Barret ◽  
Simon Raynal ◽  
Colette Jungas ◽  
Pétra Pernot ◽  
...  
Keyword(s):  
Light Scattering ◽  
Dynamic Light Scattering ◽  
Membrane Protein ◽  
Small Angle ◽  
Protein Crystallization ◽  
X Ray ◽  
X Ray Scattering ◽  
Membrane Protein Crystallization ◽  
Surfactant Phase ◽  
Ray Scattering

The structural and interactive properties of two novel hemifluorinated surfactants, F2H9-β-M and F4H5-β-M, the syntheses of which were based on the structure and hydrophobicity of the well known dodecyl-β-maltoside (DD-β-M), are described. The shape of their micellar assemblies was characterized by small-angle X-ray scattering and their intermicellar interactions in crystallizing conditions were measured by dynamic light scattering. Such information is essential for surfactant phase-diagram determination and membrane-protein crystallization.

An Integrated Study of Small-Angle X-ray Scattering and Dynamic Light Scattering on Cylindrical Micelles of Sodium Glycodeoxycholate

2004 ◽  
Vol 108 (9) ◽  
pp. 3078-3085 ◽  
Author(s):  
Luciano Galantini ◽  
Edoardo Giglio ◽  
Antonio Leonelli ◽  
Nicolae Viorel Pavel
Keyword(s):  
Light Scattering ◽  
Dynamic Light Scattering ◽  
Small Angle ◽  
X Ray ◽  
X Ray Scattering ◽  
Cylindrical Micelles ◽  
Integrated Study ◽  
Ray Scattering

Comb-like poly(4-vilylpyridinium) salts with dodecylsulfate, sodium bis(2-ethylhexyl) sulfosuccinate and bromide counter ions. Small-angle X-ray scattering and dynamic light scattering study

Polymer ◽  
2010 ◽  
Vol 51 (1) ◽  
pp. 122-128 ◽  
Author(s):  
Sergey G. Starodubtsev ◽  
Tatyana V. Laptinskaya ◽  
Alena S. Yesakova ◽  
Alexei R. Khokhlov ◽  
Eleonora V. Shtykova ◽  
...  
Keyword(s):  
Light Scattering ◽  
Dynamic Light Scattering ◽  
Small Angle ◽  
X Ray ◽  
X Ray Scattering ◽  
Counter Ions ◽  
Scattering Study ◽  
Ray Scattering

scholarly journals A General Small-Angle X-ray Scattering-Based Screening Protocol for Studying Physical Stability of Protein Formulations

Pharmaceutics ◽  
2021 ◽  
Vol 14 (1) ◽  
pp. 69
Author(s):  
Fangrong Zhang ◽  
Gesa Richter ◽  
Benjamin Bourgeois ◽  
Emil Spreitzer ◽  
Armin Moser ◽  
...  
Keyword(s):  
Light Scattering ◽  
Dynamic Light Scattering ◽  
High Throughput ◽  
Small Angle ◽  
X Ray ◽  
Sensitive Measure ◽  
X Ray Scattering ◽  
Protein Formulations ◽  
Protein Particle ◽  
Ray Scattering

A fundamental step in developing a protein drug is the selection of a stable storage formulation that ensures efficacy of the drug and inhibits physiochemical degradation or aggregation. Here, we designed and evaluated a general workflow for screening of protein formulations based on small-angle X-ray scattering (SAXS). Our SAXS pipeline combines automated sample handling, temperature control, and fast data analysis and provides protein particle interaction information. SAXS, together with different methods including turbidity analysis, dynamic light scattering (DLS), and SDS-PAGE measurements, were used to obtain different parameters to provide high throughput screenings. Using a set of model proteins and biopharmaceuticals, we show that SAXS is complementary to dynamic light scattering (DLS), which is widely used in biopharmaceutical research and industry. We found that, compared to DLS, SAXS can provide a more sensitive measure for protein particle interactions, such as protein aggregation and repulsion. Moreover, we show that SAXS is compatible with a broader range of buffers, excipients, and protein concentrations and that in situ SAXS provides a sensitive measure for long-term protein stability. This workflow can enable future high-throughput analysis of proteins and biopharmaceuticals and can be integrated with well-established complementary physicochemical analysis pipelines in (biopharmaceutical) research and industry.

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