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pH-depended protein shell dis- and reassembly of ferritin nanoparticles revealed by atomic force microscopy

Stühn, Lukas and Auernhammer, Julia and Dietz, Christian (2019):
pH-depended protein shell dis- and reassembly of ferritin nanoparticles revealed by atomic force microscopy.
In: Scientific Reports, (1), 9. Springer Nature, e-ISSN 2045-2322,
DOI: 10.25534/tuprints-00009681,
[Online-Edition: https://tuprints.ulb.tu-darmstadt.de/9681],
Secondary publishing via sponsored Golden Open Access, [Article]

Abstract

Ferritin, a protein that is present in the human body for a controlled iron storage and release, consists of a ferrihydrite core and a protein shell. Apoferritin, the empty shell of ferritin, can be modified to carry tailored properties exploitable for targeted and direct drug delivery. This protein shell has the ability to dis- and reassemble depending on the pH value of the liquid environment and can thus be filled with the desired substance. Here we observed the dis- and reassembly process of the protein shell of ferritin and apoferritin in situ and in real space using atomic force microscopy. Ferritin and apoferritin nanoparticles adsorbed on a mica substrate exhibited a change in their size by varying the pH value of the surrounding medium. Lowering the pH value of the solution led to a decrease in size of the nanoparticles whereas a successive increase of the pH value increased the particle size again. The pH dependent change in size could be related to the dis- and reassembling of the protein shell of ferritin and apoferritin. Supplementary imaging by bimodal magnetic force microscopy of ferritin molecules accomplished in air revealed a polygonal shape of the core and a three-fold symmetry of the protein shell providing valuable information about the substructure of the nanoparticles.

Item Type: Article
Erschienen: 2019
Creators: Stühn, Lukas and Auernhammer, Julia and Dietz, Christian
Title: pH-depended protein shell dis- and reassembly of ferritin nanoparticles revealed by atomic force microscopy
Language: English
Abstract:

Ferritin, a protein that is present in the human body for a controlled iron storage and release, consists of a ferrihydrite core and a protein shell. Apoferritin, the empty shell of ferritin, can be modified to carry tailored properties exploitable for targeted and direct drug delivery. This protein shell has the ability to dis- and reassemble depending on the pH value of the liquid environment and can thus be filled with the desired substance. Here we observed the dis- and reassembly process of the protein shell of ferritin and apoferritin in situ and in real space using atomic force microscopy. Ferritin and apoferritin nanoparticles adsorbed on a mica substrate exhibited a change in their size by varying the pH value of the surrounding medium. Lowering the pH value of the solution led to a decrease in size of the nanoparticles whereas a successive increase of the pH value increased the particle size again. The pH dependent change in size could be related to the dis- and reassembling of the protein shell of ferritin and apoferritin. Supplementary imaging by bimodal magnetic force microscopy of ferritin molecules accomplished in air revealed a polygonal shape of the core and a three-fold symmetry of the protein shell providing valuable information about the substructure of the nanoparticles.

Journal or Publication Title: Scientific Reports
Number: 1
Publisher: Springer Nature
Divisions: 11 Department of Materials and Earth Sciences
11 Department of Materials and Earth Sciences > Material Science
11 Department of Materials and Earth Sciences > Material Science > Physics of Surfaces
Date Deposited: 15 Dec 2019 20:56
DOI: 10.25534/tuprints-00009681
Official URL: https://tuprints.ulb.tu-darmstadt.de/9681
URN: urn:nbn:de:tuda-tuprints-96816
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