Using magnetic nanoparticles to probe protein damage in ferritin caused by freeze concentration | Zendy

E. F. Chagas | Zendy; Sara Correia Carreira | Zendy; W. Schwarzacher | Zendy

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Using magnetic nanoparticles to probe protein damage in ferritin caused by freeze concentration

Author(s) -

E. F. Chagas,

Sara Correia Carreira,

W. Schwarzacher

Publication year - 2015

Publication title -

aip advances

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.421

H-Index - 58

ISSN - 2158-3226

DOI - 10.1063/1.4935261

Subject(s) - dynamic light scattering , hydrodynamic radius , ferrofluid , glycerol , magnetization , viscosity , radius , magnetite , magnetic nanoparticles , nanoparticle , ferritin , materials science , relaxation (psychology) , chemistry , light scattering , brownian motion , analytical chemistry (journal) , magnetic field , scattering , chromatography , nanotechnology , optics , physics , biochemistry , composite material , social psychology , psychology , computer security , quantum mechanics , computer science , metallurgy

We demonstrate a method for monitoring the damage caused to a protein during freeze-thawing in the presence of glycerol, a cryo-protectant. For this work we synthesized magnetite nanoparticles doped with 2.5% cobalt inside the protein ferritin (CMF), dissolved them in different concentration glycerol solutions and measured their magnetization after freezing in a high applied field (5 T). As the temperature was raised, a step-like decrease in the sample magnetization was observed, corresponding to the onset of Brownian relaxation as the viscosity of the freeze-concentrated glycerol solution decreased. The position of the step reveals changes to the protein hydrodynamic radius that we attribute to protein unfolding, while its height depends on how much protein is trapped by ice during freeze concentration. Changes to the protein hydrodynamic radius are confirmed by dynamic light scattering (DLS) measurements, but unlike DLS, the magnetic measurements can provide hydrodynamic data while the solution remains ...

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