Bulletin of the American Physical Society
2018 Annual Meeting of the APS Mid-Atlantic Section
Volume 63, Number 20
Friday–Sunday, November 9–11, 2018; College Park, Maryland
Session B01: Poster Session (Day 1)
8:00 PM,
Friday, November 9, 2018
Edward St. John
Room: Lounge
Chair: Wendell T. Hill, III, University of Maryland, College Park
Abstract ID: BAPS.2018.MAS.B01.35
Abstract: B01.00035 : Comparative Studies of the Superparamagnetic Properties of Engineered H-rich and L-rich Human Ferritins Reconstituted with 500 57Fe-atoms / Protein
Presenter:
Thomas Longo
(Department of Physics, Villanova University, USA)
Authors:
Thomas Longo
(Department of Physics, Villanova University, USA)
Lauren Hurley
(Department of Physics, Villanova University, USA)
Kaixuan Ji
(Department of Physics, Villanova University, USA)
Lara Varden
(Department of Chemistry, SUNY Potsdam, USA)
Britannia Smith
(Department of Chemistry, SUNY Potsdam, USA)
Fadi Bou-Abdallah
(Department of Chemistry, SUNY Potsdam, USA)
Paolo Arosio
(Faculty of Medicine, University of Brescia, Italy)
Arthur Viescas
(Department of Physics, Villanova University, USA)
Georgia Papaefthymiou
(Department of Physics, Villanova University, USA)
Ferritin, the iron storage protein, consists of an inorganic ferrihydrite core surrounded by an organic protein shell, and in humans, it is found in the liver, spleen, brain, and heart. The shell consists of 24 amino acid subunits of two types: heavy (H) and light (L). In the liver and spleen, it is L-rich, while in the brain and heart it is H-rich. Since iron deposits in the brain have been linked to neurodegenerative diseases, like Parkinson’s and Alzheimer's, it is important to study the structure/function relations in these types of ferritin. Thus, we used Mӧssbauer Spectroscopy (MS) to analyze the physical properties of the cores within L-rich and an H-rich human ferritin. The MS signatures obtained in the temperature range of 4.2 < T < 300K show that magnetic spitting of the L-rich core collapses to a quadrupole doublet at a higher temperature (TB=21K) than the H-rich core (TB=11K). We used the Néel uniaxial magnetic anisotropy model for spin-relaxation-time processes in magnetic nanoparticles to extract information on core size. We found that H-rich proteins tend to form smaller cores with a larger surface-to-volume ratio, favoring high iron trafficking; while L-rich proteins form larger cores with a smaller surface-to-volume ratio, favoring long-term storage.
To cite this abstract, use the following reference: http://meetings.aps.org/link/BAPS.2018.MAS.B01.35
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