Comparative study on low resolution structures of apoferritin via SANS and SAXS

Куклин, А. И.; Murugova, T. N.; Ivankov, Oleksandr I.; Rogachev, Andrey; Soloviov, Dmytro; Kovalev, Yu. S.; Ищенко, А. В.; Zhigunov, Alexander; Куркин, Т. С.; Gordeliy, Valentin

doi:10.1088/1742-6596/351/1/012009

Cited by 9 publications

(10 citation statements)

References 22 publications

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“…These values and the estimates of ðrÞ shown are in good agreement with previous measurements and analysis of small-angle scattering from apoferritin (e.g. Kuklin et al, 2012, or the GNOM results at the data bank web site).…”

Section: Experimental Datasupporting

confidence: 90%

Estimation of the density distribution from small-angle scattering data

Hansen

2016

J Appl Cryst

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The one-dimensional density distribution for symmetrical scatterers is estimated from small-angle scattering data. The symmetry of the scatterers may be one dimensional (lamellar), two dimensional (cylindrical) or three dimensional (spherical). Previously this problem has been treated either by a two-step approach with the distance distribution as an intermediate [Glatter (1981).J. Appl. Cryst.14, 101–108] or in a single step using spherical harmonics [Svergun, Feigin & Schedrin (1982).Acta Cryst.A38, 827–835]. A combination of these two methods is presented here, where the density distribution is estimated using constraints without the explicit use of an intermediate distribution. A maximum entropy constraint is introduced for this problem and the results are compared with the results of the conventional smoothness constraint. Bayesian methods are used for estimation of the overall noise level of the experimental data and for the maximum dimension of the density distribution. The method described is tested on both simulated and experimental data and shown to provide reliable estimates for the Guinier radius and maximum dimension. In both cases the effects of minor deviations from the assumed symmetry as well as incorrect background subtraction are studied.

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Section: Experimental Datasupporting

confidence: 90%

Estimation of the density distribution from small-angle scattering data

Hansen

2016

J Appl Cryst

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“…44 61 62 Ferritin is a spherical hollow protein cage with internal and external diameter of about 120 Å and 75 Å, respectively. 63 It can accumulate and store approximately 4500 iron atoms. The apoferritin protein cage is composed of 80-90% of L-chain (light chain) and 10-20% of H-chain (heavy chain) subunits with 55% sequence homology.…”

Section: Structure Of Ferritinmentioning

confidence: 99%

Ferritin Nanocages: A Novel Platform for Biomedical Applications

Bhushan¹,

Su²,

Matai³

et al. 2014

j biomed nanotechnol

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Ferritin is a ubiquitous iron storage protein responsible for maintaining the iron homeostasis in living organism and thereby protects the cell from oxidative damage. The ferritin protein cages have been used as a reaction vessel for the synthesis of various non-native metallic nanoparticles inside its core and also used as a nanocarrier for various applications. Lack of suitable non-viral carrier for targeted delivery of anticancer drugs and imaging agents is the major problem in cancer therapy and diagnosis. The pH dependent reversible assembling and disassembling property of ferritin renders it as a suitable candidate for encapsulating a variety of anticancer drugs and imaging probes. Ferritins external surface is chemically and genetically modifiable which can serve as attachment site for tumor specific targeting peptides or moieties. Recent studies, further establishes ferritin as a multifunctional nanocarrier for targeted cancer diagnosis and therapy. Moreover, the biological origin of these protein cages makes it a biocompatible nanocarrier that stabilizes and protects the enclosed particles from the external environment without provoking any toxic or immunogenic responses. This review mainly focuses on the application of ferritin nanocages as a novel non-viral nanocarrier for cancer therapy and it also highlights various biomedical applications of ferritin nanocages.

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“…1. The scattering curve of apoferritin (LF = 0) is well described by the form-factor of a monodisperse spherical shell [22,23]:…”

Section: Saxs and Sans Data Analysis At Full Contrastmentioning

confidence: 99%

Effect of iron oxide loading on magnetoferritin structure in solution as revealed by SAXS and SANS

Melníková

Петренко

Авдеев

et al. 2014

Colloids and Surfaces B: Biointerfaces

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Synthetic biological macromolecule of magnetoferritin containing an iron oxide core inside a protein shell (apoferritin) is prepared with different content of iron. Its structure in aqueous solution is analyzed by small-angle synchrotron X-ray (SAXS) and neutron (SANS) scattering.The loading factor (LF) defined as the average number of iron atoms per protein is varied up to LF=800. With an increase of the LF, the scattering curves exhibit a relative increase in the total scattered intensity, a partial smearing and a shift of the match point in the SANS contrast variation data. The analysis shows an increase in the polydispersity of the proteins and a corresponding effective increase in the relative content of magnetic material against the protein moiety of the shell with the LF growth. At LFs above ~150, the apoferritin shell undergoes structural changes, which is strongly indicative of the fact that the shell stability is affected by iron oxide presence.

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Comparative study on low resolution structures of apoferritin via SANS and SAXS

Cited by 9 publications

References 22 publications

Estimation of the density distribution from small-angle scattering data

Estimation of the density distribution from small-angle scattering data

Ferritin Nanocages: A Novel Platform for Biomedical Applications

Effect of iron oxide loading on magnetoferritin structure in solution as revealed by SAXS and SANS

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