Dynamics of encapsulated hepatitis B surface antigen

Rasmussen, Martin Kaag; Pereira, Jose E. M.; Berg, M.C.; Iles, Gail N.; Souza, Nicolas R. de; Jalarvo, Niina; Botosso, Viviane Fongaro; Sant’Anna, Osvaldo A.; Fantini, M.C.A.; Bordallo, Heloisa N.

doi:10.1140/epjst/e2019-700103-x

Cited by 8 publications

(12 citation statements)

References 17 publications

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“…Our previous works explained in detail how the complementary techniques, such as NAI, scanning electron microscopy (SEM) with energy-dispersive X-ray spectroscopy (EDS) and transmission electron microscopy (TEM), dynamic light scattering (DLS), thermogravimetric analysis (TGA), synchrotron radiation circular dichroism (SRCD) and intrinsic tryptophan fluorescence spectroscopies, were used to further evaluate the effectiveness of our strategies to develop oral vaccines, including biological assays. Thus, these results will not be detailed here, we refer the reader to the literature (Carvalho et topical reviews , 2010;Mariano-Neto et al, 2014;Scaramuzzi et al, 2016;Garcia et al, 2016;Lopes et al, 2019;Mercuri et al, 2006;Rasmussen et al, 2019bRasmussen et al, , 2021. These applications will be described and correlated in the Discussion.…”

Section: Materials Characterizationmentioning

confidence: 98%

Using crystallography tools to improve vaccine formulations

Fantini

Oliveira

Lopes

et al. 2021

Int Union Crystallogr J

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This article summarizes developments attained in oral vaccine formulations based on the encapsulation of antigen proteins inside porous silica matrices. These vaccine vehicles show great efficacy in protecting the proteins from the harsh acidic stomach medium, allowing the Peyer's patches in the small intestine to be reached and consequently enhancing immunity. Focusing on the pioneering research conducted at the Butantan Institute in Brazil, the optimization of the antigen encapsulation yield is reported, as well as their distribution inside the meso- and macroporous network of the porous silica. As the development of vaccines requires proper inclusion of antigens in the antibody cells, X-ray crystallography is one of the most commonly used techniques to unveil the structure of antibody-combining sites with protein antigens. Thus structural characterization and modelling of pure antigen structures, showing different dimensions, as well as their complexes, such as silica with encapsulated hepatitis B virus-like particles and diphtheria anatoxin, were performed using small-angle X-ray scattering, X-ray absorption spectroscopy, X-ray phase contrast tomography, and neutron and X-ray imaging. By combining crystallography with dynamic light scattering and transmission electron microscopy, a clearer picture of the proposed vaccine complexes is shown. Additionally, the stability of the immunogenic complex at different pH values and temperatures was checked and the efficacy of the proposed oral immunogenic complex was demonstrated. The latter was obtained by comparing the antibodies in mice with variable high and low antibody responses.

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Section: Materials Characterizationmentioning

confidence: 98%

Using crystallography tools to improve vaccine formulations

Fantini

Oliveira

Lopes

et al. 2021

Int Union Crystallogr J

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“…Active matter and driven matter generally exhibit self-assembled or self-organized dynamic structures. Examples of these phenomena are given in the papers by Rasmussen et al [1], Doostmohammadi and Yeomans [2], Horowitz et al [3] and Helgesen [4] in this issue.…”

mentioning

confidence: 95%

Physics inspired by living matter: dynamics, topology and functionality

Skjeltorp

Helgesen

2019

Eur. Phys. J. Spec. Top.

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“…An excellent experimental tool for describing such complex water interactions on multiple length and time scales is quasielastic neutron scattering (QENS). Here, QENS is an ideal tool due to the neutron's natural scattering sensitivity [4][5][6] and scattering length density contrast between H and D [7]. QENS further allows to study motions in the time region of 10 −9 to 10 −13 s, while monitoring such motions in space from 0.1 to 10 nm [8,9].…”

Section: Introductionmentioning

confidence: 99%

“…In QENS experiments these variables are the positions of the H-atoms in time. Additionally, the neutron's natural scattering contrast between hydrogen (H) and deuterium (H2, D), both in magnitude and phase, provides for an extraordinary method for highlighting (or hiding) H-containing components in complex systems [5], making neutron scattering especially successful for studies of structural characteristics [11] and dynamics of confined water [3,4,[6][7][8][12][13][14]. Furthermore, QENS is the only spectroscopic technique that provides information on the dynamics and atomic-motion amplitudes over a predetermined length scale [15][16][17].…”

Section: Introductionmentioning

confidence: 99%

“…The challenge here is the lack of accuracy of the interatomic potentials, hampering real predictive modelling of atomic-scale dynamics in time [23]. While on the other, the complexity of such process makes the analysis, interpretation, and modeling of QENS data difficult [3,6,16]. Usually in QENS analysis, empirical models for special atomic motion types are used to extract diffusion coefficients and mean-square displacements [24,25].…”

Section: Introductionmentioning

confidence: 99%

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Uncovering the Dynamics of Confined Water Using Neutron Scattering: Perspectives

Bordallo

Kneller

2022

Front. Phys.

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The main characteristic of liquid water is the formation of dynamic hydrogen bond networks that occur over a broad range of time scales from tens of femtoseconds to picoseconds and are responsible for water’s unique properties. However, in many important processes water does not exist in its bulk form, but in confined nanometer scale environments. The investigation of this confined water dynamics is challenging since the intermediate strength of the hydrogen bonds makes it possible to alter the structure and dynamics of this constrained water. Even if no single experimental technique can give a full picture of such intricate dynamics, it is well established that quasielastic neutron scattering (QENS) is a powerful tool to study the modification of hydrogen bonds in confinement in various materials. This is possible because neutrons tell us where the atoms are and what they are doing, can detect hydrogen, are penetrative and non-destructive. Furthermore, QENS is the only spectroscopic technique that provides information on the dynamics and atomic-motion amplitudes over a predetermined length scale. However scientific value of these data is hardly exploited and never to its full potential. This perspective highlights how new developments on instrumentation and data analysis will lead to appreciable progress in our understanding of the dynamics of complex systems, ranging from biological organisms to cloud formation.

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Dynamics of encapsulated hepatitis B surface antigen

Cited by 8 publications

References 17 publications

Using crystallography tools to improve vaccine formulations

Using crystallography tools to improve vaccine formulations

Physics inspired by living matter: dynamics, topology and functionality

Uncovering the Dynamics of Confined Water Using Neutron Scattering: Perspectives

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