Structural Evolution of Aqueous Zirconium Acetate by Time-Resolved Small-Angle X-ray Scattering and Rheology

2015 ◽  
Vol 119 (22) ◽  
pp. 12660-12667 ◽  
Author(s):  
Martin Bremholm ◽  
Henrik Birkedal ◽  
Bo Brummerstedt Iversen ◽  
Jan Skov Pedersen
Keyword(s):  
Small Angle ◽  
Structural Evolution ◽  
Time Resolved ◽  
X Ray ◽  
Zirconium Acetate ◽  
X Ray Scattering ◽  
Ray Scattering

In situ Time-Resolved Small-Angle X-ray Scattering Reveals the Formation Kinetics of Polyelectrolyte Complex Micelles

2019 ◽  
Author(s):  
Hao Wu ◽  
Jeffrey Ting ◽  
Siqi Meng ◽  
Matthew Tirrell
Keyword(s):  
Small Angle ◽  
Self Assembly ◽  
Electrostatic Interactions ◽  
Polyelectrolyte Complex ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Kinetics Of ◽  
Ray Scattering

We have directly observed the <i>in situ</i> self-assembly kinetics of polyelectrolyte complex (PEC) micelles by synchrotron time-resolved small-angle X-ray scattering, equipped with a stopped-flow device that provides millisecond temporal resolution. This work has elucidated one general kinetic pathway for the process of PEC micelle formation, which provides useful physical insights for increasing our fundamental understanding of complexation and self-assembly dynamics driven by electrostatic interactions that occur on ultrafast timescales.

scholarly journals Osmotic shrinkage of sterically stabilized liposomes as revealed by time-resolved small-angle X-ray scattering

2014 ◽  
Vol 47 (1) ◽  
pp. 35-40 ◽  
Author(s):  
Zoltán Varga ◽  
András Wacha ◽  
Attila Bóta
Keyword(s):  
Form Factor ◽  
Small Angle ◽  
Freeze Fracture ◽  
Initial Step ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Sterically Stabilized Liposomes ◽  
Liposome Size ◽  
Ray Scattering

Time-resolved synchrotron small-angle X-ray scattering (SAXS) was used to study the structural changes during the osmotic shrinkage of a pharmacologically relevant liposomal drug delivery system. Sterically stabilized liposomes (SSLs) with a diameter of 100 nm and composed of hydrogenated soy phosphocholine, cholesterol and distearoyl-phosphoethanolamine-PEG 2000 prepared in a salt-free buffer were mixed with a buffered 0.3 MNaCl solution using a stopped flow apparatus. The changes in the liposome size and the bilayer structure were followed by using SAXS with a time resolution of 20 ms. A linear decrease in liposome size is observed during the first ∼4 s of the osmotic shrinkage, which reveals a water permeability value of 0.215 (15) µm s−1. The change in the size of the liposomes upon the osmotic shrinkage is also confirmed by dynamic light scattering. After this initial step, broad correlation peaks appear on the SAXS curves in theqrange of the bilayer form factor, which indicates the formation of bi- or oligolamellar structures. Freeze-fracture combined with transmission electron microscopy revealed that lens-shaped liposomes are formed during the shrinkage, which account for the appearance of the quasi-Bragg peaks superimposed on the bilayer form factor. On the basis of these observations, it is proposed that the osmotic shrinkage of SSLs is a two-step process: in the initial step, the liposome shrinks in size, while the area/lipid adapts to the decreased surface area, which is then followed by the deformation of the spherical liposomes into lens-shaped vesicles.

Time-resolved isothermal crystallization of absorbable PGA-co-PLA copolymer by synchrotron small-angle X-ray scattering and wide-angle X-ray diffraction

Polymer ◽  
2001 ◽  
Vol 42 (21) ◽  
pp. 8965-8973 ◽  
Author(s):  
Zhi-Gang Wang ◽  
Xuehui Wang ◽  
Benjamin S. Hsiao ◽  
Saša Andjelić ◽  
Dennis Jamiolkowski ◽  
...  
Keyword(s):  
Small Angle ◽  
Isothermal Crystallization ◽  
Wide Angle ◽  
X Ray Diffraction ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

Time-Resolved Small-Angle X-ray Scattering Study of the Folding Dynamics of Barnase

2011 ◽  
Vol 405 (5) ◽  
pp. 1284-1294 ◽  
Author(s):  
Tsuyoshi Konuma ◽  
Tetsunari Kimura ◽  
Shuzo Matsumoto ◽  
Yuji Goto ◽  
Tetsuro Fujisawa ◽  
...  
Keyword(s):  
Small Angle ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Folding Dynamics ◽  
Scattering Study ◽  
Ray Scattering

scholarly journals Visualizing a viral genome with contrast variation small angle X-ray scattering

2020 ◽  
Vol 295 (47) ◽  
pp. 15923-15932
Author(s):  
Josue San Emeterio ◽  
Lois Pollack
Keyword(s):  
Small Angle ◽  
Viral Genome ◽  
Viral Assembly ◽  
Measured Signal ◽  
Structural Rearrangements ◽  
Contrast Variation ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

Despite the threat to human health posed by some single-stranded RNA viruses, little is understood about their assembly. The goal of this work is to introduce a new tool for watching an RNA genome direct its own packaging and encapsidation by proteins. Contrast variation small-angle X-ray scattering (CV-SAXS) is a powerful tool with the potential to monitor the changing structure of a viral RNA through this assembly process. The proteins, though present, do not contribute to the measured signal. As a first step in assessing the feasibility of viral genome studies, the structure of encapsidated MS2 RNA was exclusively detected with CV-SAXS and compared with a structure derived from asymmetric cryo-EM reconstructions. Additional comparisons with free RNA highlight the significant structural rearrangements induced by capsid proteins and invite the application of time-resolved CV-SAXS to reveal interactions that result in efficient viral assembly.

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